Post on 07-Feb-2020
Hierarchical Classification of Glycoside HydrolasesDaniil G. Naumoff
Laboratory of BioinformaticsState Institute for Genetics and Selection of Industrial Microorganisms
Moscow, Russiahttp://bioinform.genetika.ru/members/Naumoff/index.htm
Gos NII Genetika
Moscow, Russia
Иерархическая классификация гликозил- гидролаз
Даниил Геннадиевич НаумовЛаборатория биоинформатики
Государственный Научно-Исследовательский Институт Генетики и СелекцииПромышленных Микроорганизмов, Москва
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Enzyme Classification (IUBMB)EC 1 – OxidoreductasesEC 2 – Transferases
EC 2.4 – Glycosyltransferases (including transglycosidases)EC 2.4.1 – Hexosyltransferases
EC 2.4.1.10 – Levansucrase (β-fructosyltransferase)EC 2.4.1.67 – Galactinol-raffinose galactosyltransferase
EC 2.4.2 – PentosyltransferasesEC 3 – Hydrolases
EC 3.2 – Glycosylases (glycoside hydrolases)EC 3.2.1 – O- and S-Glycosylases
EC 3.2.1.20 – Maltase (a-glucosidase)EC 3.2.1.22 – Melibiase (a-galactosidase)EC 3.2.1.26 – Sucrase (invertase, β-fructofuranosidase)
EC 3.2.2 – N-GlycosylasesEC 4 – LyasesEC 5 – IsomerasesEC 6 – Ligases
Glycoside Hydrolases = EC 3.2.1.X; X=1…>200
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Progress in the Sequence Based Classification ofGlycoside Hydrolases and Their Homologues
CAZy = the Carbohydrate-Active enZYmes server (http://www.cazy.org/CAZY)
Number ofproteins
Number of families Reference
300 36 Henrissat. Biochem. J. 1991, 280:309-316
480 45 Henrissat & Bairoch. Biochem. J. 1993, 293:781-788
950 57 (17 => 5 clans) Henrissat & Bairoch. Biochem. J. 1996, 316:695-696
… 62 (19 => 5 clans) Henrissat & Davies. Curr. Opin. Struct. Biol. 1997, 7:637-644
2.200 70 (…) Coutinho & Henrissat. CAZy server. 1998
>20.000 101 (46 => 14 clans) Coutinho & Henrissat. CAZy server. 2005
~30.000 106 (46 => 14 clans) Coutinho & Henrissat. CAZy server. 2006
>30.000 110 (46 => 14 clans) Coutinho & Henrissat. CAZy server. 2007
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Sequence Based Classification of Glycoside Hydrolasesthe Carbohydrate-Active Enzymes (CAZy) server (www.cazy.org/CAZY/)
• 30.000 protein sequences => 105 families (GH1-GH110, except GH21, GH40, GH41, GH60, and GH69)• 46 glycoside hydrolase families => 14 clans (GH-A–GH-N)
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(β)3-solenoidinversion (axial orientation)28, 49GH-N(a/a)6inversion (equatorial orientation)8, 48GH-M(a/a)6inversion (axial orientation)15, 65GH-L(β/a)8 -barrelretention (equatorial orientation)18, 20GH-K5-fold β-propellerretention (β-furanoside)32, 68GH-Ja+βinversion (equatorial orientation)24, 46, 80GH-I(β/a)8 -barrelretention (axial orientation)13, 70, 77GH-HNot knowninversion (axial orientation)37, 63GH-G5-fold β-propellerinversion (equatorial orientation)43, 62GH-F6-fold β-propellerretention (equatorial orientation)33, 34, 83GH-E(β/a)8 -barrelretention (axial orientation)27, 36GH-Dβ-jelly rollretention (equatorial orientation)11, 12GH-Cβ-jelly rollretention (equatorial orientation)7, 16GH-B
(β/a)8 -barrelretention (equatorial orientation)1, 2, 5, 10, 17, 26, 30, 35, 39,42, 50, 51, 53, 59, 72, 79, 86
GH-A
Tertiary StructureOptical ConfigurationFamilies (GH)Clan
Clans of Glycoside HydrolasesClic
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Common name: α-galactosidase
Reaction: Hydrolysis of terminal, non-reducing α-D-galactose residues in α-D-galactosides,including galactose oligosaccharides, galactomannans, and galactolipids
Molecular mechanism of hydrolyzing reaction: double displacement with overall retention ofthe anomeric configuration of the axial glycosidic bond
Other names: melibiase; α-D-galactosidase; α-galactosidase A; α-D-galactosidegalactohydrolase; α-galactoside galactohydrolase
Systematic name: α-D-galactoside galactohydrolase
Comments: Also hydrolyses α-D-fucosides
EC 3.2.1.22
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GH4 – α-galactosidase from Escherichia coli and bifunctional enzymes with α-galactosidase andα-glucosidase (EC 3.2.1.20) activities from Thermotoga maritime and Thermotoga neapolitana
+ 6-phospho-α-glucosidases (EC 3.2.1.122) from Eubacteria+ 6-phospho-β-glucosidases (EC 3.2.1.86) from Eubacteria
GH27 – mainly α-galactosidases from Eukaryota (animals, plants, fungi, etc.) and some Eubacteria+ α-N-acetylgalactosaminidases (EC 3.2.1.49) from Eukaryota (animals and fungi)+ isomalto-dextranase (EC 3.2.1.94) from Arthrobacter globiformis
GH36 – mainly α-galactosidases from Eubacteria and Eukaryota (fungi and plants)+ α-galactosyltransferases (EC 2.4.1.67 and EC 2.4.1.82) from plants+ α-N-acetylgalactosaminidase from Clostridium perfringens+ ORFs from Sulfolobus solfataricus and Sulfolobus tokodaii
GH57 – α-galactosidases from Pyrococcus furiosus and Thermococcus alcaliphilus+ α-amylases (EC 3.2.1.1), amylopullulanase (EC 3.2.1.41), and
4-α-glucanotransferases (EC 2.4.1.x) from Eubacteria and ArchaeaGH110 – α-galactosidase from Bacteroides fragilis
Glycoside hydrolase families, which include α-galactosidases
clanGH-D
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Subfamily 27a:
– plant α-galactosidases: Arabidopsis, Carica, Coffea, Cyamopsis, Glycine, Helianthus, Hordeum, Lycopersicon, Oryza, Petunia,Phaseolus, and Senna
– α-galactosyltransferase from Ajuga reptans
– animal α-galactosidases and α-N-acetylgalactosaminidases: Anopheles, Apis, Ateles, Brugia, Caenorhabditis, Ciona, Danio,Drosophila, Gallus, Homo, Mus, Rattus, Takifugu, and Tetraodon
– fungal and yeast α-galactosidases: Aspergillus, Ganoderma, Gibberella, Magnaporthe, Mortierella, Penicillium, Phanerochaete,Saccharomyces, Schizosaccharomyces, Thermomyces, Torulaspora, Trichoderma, Ustilago, and Zygosaccharomyces
– α-N-acetylgalactosaminidase from Acremonium sp.
– ORFs from Dictyostelium discoideum and Toxoplasma gondii
– bacterial α-galactosidases: Cellvibrio mixtus, Clostridium josui, Pseudomonas fluorescens, Saccharopolyspora erythraea, andStreptomyces coelicolor
– bacterial ORFs: Bacteroides, Fibrobacter, Microbulbifer, Porphyromonas, and Streptomyces
Family GH27
Subfamily 27b:
– plant ORFs: Arabidopsis thaliana and Oryza sativa
– bacterial ORFs: Bacillus halodurans, Bifidobacterium longum, Kineococcus radiotolerans, and Ruminococcus albus
Subfamily 27c:
– α-galactosidase from Trichoderma reesei
– ORF from Aspergillus nidulans
Unclassified proteins
– isomalto-dextranase from Arthrobacter globiformis
– bacterial ORFs: Bacteroides thetaiotaomicron and Streptomyces avermitilis
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Tertiary Structure of GH27 Glycosidases(Trichoderma reesei α-galactosidase)
C- terminal domain(β-sandwich fold,Greek key motif)
N-terminal catalytic(β/α)8-domain(TIM barrel-type structure)
GH27N
GH27C
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GH27N GH27C
GH27N
GH27N GH27C CBM13
GH27N GH27C CBM6
GH27N GH27C CBM6 CBM13
GH27N CBM13 GH27C
NEW1 GH27N CBM13 GH27C
NEW1 GH27N GH27C
NEW2 NEW1 GH27N GH27C
GH27N GH27C NEW3 NEW2
GH27N GH27C NEW3
GH27N GH27C Dockerin
GH27N GH27C CBM1 CE1N-terminal domain of GH27 family
C -terminal domain of GH27 family
CE1 domain of carbohydrate esterases
Carbohydrate-binding module CBM1
Carbohydrate-binding module CBM6
Carbohydrate-binding module CBM13
Dockerin I domain
Uncharacterized domain
Uncharacterized domain (NPCBM)
Uncharacterized domain
CBM13
CBM6
Dockerin
NEW1
NEW2
NEW3
CBM1
CE1
GH27C
GH27N
Domain structure of proteins of the GH27 familyaccording to Naumoff D.G. Phylogenetic analysis of α-galactosidases of the GH27 family. Molecular Biology (Engl Transl), 2004, 38(3):388-399.
PDF: http://bioinform.genetika.ru/members/Naumoff/MB2004E.pdf
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Family GH36
Subfamily GH36A:– bacterial α-galactosidases: Azotobacter, Bacillus, Geobacillus, Bifidobacterium, Carnobacterium, Clostridium, Enterococcus,
Erwinia, Escherichia, Geobacillus, Klebsiella, Lactobacillus, Lactococcus, Leuconostoc, Novosphingobium, Oenococcus,
Pediococcus, Ruminococcus, Streptococcus, Streptomyces, Thermoanaerobacter, Treponema, Vibrio, and Yersinia
– fungal α-galactosidases: Absidia, Aspergillus, Gibberella, Penicillium, and Trichoderma
Subfamily GH36B:– bacterial α-galactosidases: Burkholderia, Leptospira, Streptomyces, Thermotoga, Thermus, and Vibrio
Subfamily GH36C:– plant alkaline α-galactosidases or seed imbibition proteins: Arabidopsis, Brassica, Cicer, Cucumis, Hordeum, Lycopersicon,
Malus, Oryza, and Persea
– plant α-galactosyltransferases: Alonsoa, Arabidopsis, Cucumis, Medicago, Oryza, Pisum, Stachys, and Vigna
– fungal ORFs: Aspergillus, Coccidioides, Cryptococcus, Gibberella, Magnaporthe, Neurospora, and Ustilago
– ORF from Toxoplasma gondii
– α-galactosidase from Bifidobacterium breve
– bacterial ORFs: Bifidobacterium longum, Bacteroides fragilis, and Bacteroides thetaiotaomicron
– ORFs from Sulfolobus solfataricus and Sulfolobus tokodaii
Subfamily GH36D:– α-N-acetylgalactosaminidase from Clostridium perfringens
– bacterial ORFs: Aeromonas, Clostridium, Escherichia, Photorhabdus, and Streptococcus
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MEL1_YEAST 65 GYKYIILDDCWS 141 NRVDYLKYDNCY 204 WRMSGDV 258 WNDLDNLAGAL_PHAVU 106 GYQYINIDDCWG 184 WGIDYLKYDNCE 242 WRTTGDI 274 WNDPDMLNAGA_HUMAN 71 GYTYLNIDDCWI 148 WKVDMLKLDGCF 212 WRNYDDI 248 WNDPDMLAGL1_BIFLO 48 GWDTLVIDIDWY 178 WGLDFLKVDDMQ 240 WRISDDL 272 WADADMVAGL3_HYPJE 234 GYDLCSLDSGWQ 339 WGVDMLKLDFLT 407 MRTDQDL 451 YPDMDALIMD_ARTGO 100 GYDIACTD-GWI 219 LGVPYLRIDFLS 290 VRINADA 338 ILDGDFM
AGAL_LACPL 367 GIEMFVLDDGWF 478 VPIDYIKWDMNR 551 QSWPSDN 584 GTSPDELAGL2_HYPJE 375 GIKLFVLDDGWF 496 ASISYVKWDNNR 561 HIWTSDD 594 SAVPNGQAGL7_ASPFU 413 GAGYFVIDAGWY 524 YGVGYFKFDYNI 595 LQSSSDQ 626 WAYPQPA
AGAL_THEMA 213 PFEVFQIDDAYE 319 MGYRYFKIDFLF 382 MRIGPDT 423 LNDPDCLAGAL_VIBPA 227 DLEWVLLDDGYQ 341 WGVELFKLDANY 404 MRVSDDV 436 QIDPDCAAGL3_STRCO 329 GLKWAVLDDGWQ 438 WGYEGLKIDGQH 512 QYPSSDP 540 SYSGDHV
AGAL_SULSO 256 RLNWVIIDDGWQ 360 RDFDLVKVDNQW 421 MRNSIDY 454 YPDYDMFAGAL_BIFBR 339 PVSWVLIDDGWS 458 AGVDFVKVDSQS 523 TRTSDDF 556 HCDWDMFGALT_VIGAN 251 APRFVVIDDGWQ 476 TGVTGVKIDVIH 544 GRVGDDF 585 QPDWDMF
NAGA_CLOPE 253 TLDAFVVDDGWA 355 YDISYWKIDGML 429 IQTSQDV ...ORF1_CLOPE 515 PIDSYVVDDGWH 634 FDIDYWKLDGFA 715 IQNSQDT ...ORF1_ECOLI 297 ALDAFLLDDGWD 393 EHITSFKLDGMG 458 WRQGDDI ...
ORF2_CLOPE 112 PKGIIMIDDGWS 220 YGVDGFKFDAGD 286 HSWEYNG 344 ALMPMMQXYLQ_LACPE 297 PLDVFHFDCFWQ 406 MGVDSFKTDFGE 474 IQYTGAA 534 LLSSHSRXYLS_SULSO 250 PLDVIVLDWRYW 345 LGIDAYWLDASE 423 ISWSGDV 483 TFCPILRLYAG_HUMAN 397 PLDVQWNDLDYM 510 VPFDGMWIDMNE 611 GHWTGDV 666 AFYPFMR
GH27
GH36A
GH36B
GH36C
GH36D
GH31
Four conserved regions in proteins of the α-galactosidase superfamily, containing Asp residues
Nucleophile Donor H+
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The neighbor-joining phylogenetic tree of the α-galactosidase superfamily
GH31
XYLS SULSOAGL2 BACTQ
AGLU ACIACSUIS HUMANc
SUIS HUMANnLYAG HUMAN
5572
3859
89
XYLQ LACPEORF1 THEMA
ORF1 BACHAYICI ECOLIORF1 CLOAC
4270
4077
86
ORF1 CHLAUORF2 CLOPE
ORF1 MOUSEORF1 DROME
8036
43
69
ORF1 AERHYORF1 ECOLI
93
NAGA CLOPEORF1 STRPNORF1 CLOPE
3992
98
25
AGL3 STRCOAGL2 STRCO
AGAL THETHAGAL THET2 77
AGAL THEMAAGAL LEPIN 72
3757
24
AGAL VIBCHAGAL VIBPA 99
20
30
AGA2 PEDPEAGA1 PEDPE
AGAL LACPLAGAL STRMUAGL2 RUMAL 40
39
AGL5 BACFRAGL6 BACFR
94
54
49
AGL6 ASPFUAGLC ASPNGAGL2 HYPJE
6979
21
AGAL ABSCOAGL2 BIFLORAFA ECOLI 51
31
39
86
AGL3 RUMALAGL7 ASPFU
99
65
AGAL PORGI
MEL2 ARATHAGAL CYATEAGAL PHAVU
10061
AGAL SACERAGAL PSEFLAGAL MICDE
9716
9
AGL1 STRCOAGL2 ASPFU
AGAL FIBSUAGAL CLOJO
6716
5
AGLB ASPNGMEL1 YEASTMELA PHACH
2733
6
AGLA ASPNGNAGA ACRSP
98
MEL1 CAEELMEL1 DROME
NAGA HUMANAGAL HUMAN56
8046
48
AGL3 BACFRAGL2 BACFRAGL1 BACFR
10012
7
21
AGL3 HYPJEIMD ARTGO
MEL4 ARATHMEL5 ORYSA
94
AGL1 BIFLOAGAL BACHAAGL1 RUMAL
6247
49
3972
84
AGAL SULTOAGAL SULSO93
AGL4 BACFRAGAL BIFBR76
ORF2 ARATHSTAS PISSAGALT VIGAN67
45
ORF1 ARATHSIP CICAR
SIP HORVU5358
94
36
89
45
57
GH27
GH36C
GH36A
GH36B
GH36D
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AGAL SULSOAGL5 BACTH
AGAL BIFBRORF1 NEUCR
STAS STAAFAGA1 CUCME713
623670
519995
AGL4 STRAVIMD ARTGO
AGL8 ASPNIAGL3 HYPJE983
879532
MEL4 ARATHMEL5 ORYSA999
AGL1 BIFLOAGAL BACHAAGL1 RUMAL862
905903
410
AGL3 STRAVAGL3 BACFR
AGL4 BACTHAGL3 BACTH
996988
AGL5 BACTHNAGA ACRSP
AGL4 ASPFUAGLA ASPNG
999993
AGL2 DICDIAGAL HUMAN
MEL1 CAEELNAGA HUMANMEL1 DROME
794479996
525
616
AGL1 STRAVAGL2 STRAVAGL1 STRCO1000
906
AGAL MICDEAGAL PSEFL998
AGAL SACERAGAL FIBSUAGAL CLOJO376
479378
124
AGL1 DICDIMEL6 ORYSA
MEL2 ORYSAMEL1 ORYSA767
990265
AGAL PORGIAGL1 BACFR
AGL1 BACTHAGL2 BACFR973
1000580
AGL2 BACTHAGL2 ASPNIAGL2 ASPFU1000
AGL1 USTMAAGL2 GIBZE
AGL3 ASPFUAGL3 ASPNI1000
885689
827
MELA PHACHMEL1 UMBVI
MEL1 SCHPOAGL1 ASPFU
MEL5 YEASTMEL1 SACKL1000
515250
386975
MEL2 UMBVIAGL1 GIBZE
AGL1 HYPJEAGL1 PENPU
AGL5 ASPNIAGL1 PENSI
814554
987866
994374
421
342
466
143
76
103
57
265
372
721
513
AGLB ASPNG
27b27c
27a
1000
AGL5 ASPFU
GH36CPhylogenetic tree of
GH27 family
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Phylogenetic tree ofGH27 family
27cIMD ARTGOAGL8 ASPNIAGL3 HYPJE1000
AGL4 STRAV MEL5 ORYSAMEL4 ARATH999AGL1 RUMAL
AGL1 BIFLOAGL1 BACHA555953
944
AGL3 STRAVAGL3 BACFR
AGL3 BACTHAGL4 BACTH1000991
AGL5 BACTHNAGA ACRSP
AGL4 ASPFUAGLA ASPNG999985
AGL2 DICDIAGAL DANRE
AGAL TAKRUAGAL MOUSEAGAL HUMAN10006681000
NAGA CIOINNAGA DANRENAGA TAKRU976NAGA GALGANAGA HUMAN
NAGA RATNAGA MOUSE10001000923
1000809
MEL1 BRUMAMEL1 CAEBRMEL1 CAEEL1000981
MEL2 DROMEMEL2 ANOGA782
MEL1 ANOGAMEL1 DROME1000
913839
802
999
613
552
AGAL CLOJOAGAL FIBSU220
AGAL PSEFLAGAL MICDE1000
AGAL SACERAGL1 STRAV
AGL1 STRCOAGL2 STRAV1000874
42480
51
AGL1 DICDI MEL2 ARATHMEL6 ORYSAMEL4 ORYSA10001000
MEL3 ORYSAMEL2 ORYSA
AGAL CARPAMEL3 ARATH1000897746
MEL1 ORYSAAGAL HELAN
MEL1 ARATHAGAL LYCESAGAL COFAR399
AGAL SENOCAGAL CYATE
AGAL GLYMAAGAL PHAVU1000597
977233
373732988
579
999
404
AGL2 BACTHAGAL PORGI
AGL1 BACFRAGL1 BACTHAGL2 BACFR8311000514334
AGL2 ASPNIAGL2 ASPFU1000
AGL1 USTMAAGL2 GIBZE
AGL3 ASPFUAGL3 ASPNI1000955
663578
AGL1 GIBZEAGL1 HYPJE
AGL1 PENPUAGL1 PENSI
AGL5 ASPNIAGL5 ASPFUAGLB ASPNG763529
997939
1000727
MEL2 UMBVIMELA PHACH
MEL1 UMBVIMEL1 SCHPO
AGL1 ASPFUMEL4 SACKLMEL1 SACKL1000
MELC YEASTMELR YEAST
MELT YEASTMELP YEASTMEL5 YEAST782MELJ YEAST
MELD YEASTMELX YEAST958842
998630
978696
1000958
556388
950
474
508
170
250
343
352
919
397
6441000
50
27b
I
II
III
IV
27a
468
630
1000
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Families of the α-galactosidase superfamily and family GH97Family GH27 GH31 GH36A GH36B GH36C GH36D GH97Clan GH-D None GH-D GH-D GH-D GH-D None
COG1501KOG1065
EC 2.4.1.x EC 2.4.1.x EC 2.4.1.67EC 3.2.1.22 EC 3.2.1.3 EC 2.4.1.82EC 3.2.1.49 EC 3.2.1.10 EC 3.2.1.22EC 3.2.1.94 EC 3.2.1.20
EC 3.2.1.48EC 4.2.2.13
Molecularmechanism
Retaining Retaining Retaining Not known Not known Not known Not known
Eukaryota: Eukaryota: Eukaryota: Eubacteria: Eukaryota: Eubacteria: Eukaryota:Alveolata Alveolata Fungi Acidobacteria Alveolata Firmicutes Metazoa (?)
FungiEntamoebidae
Eubacteria:
Proteobacteria
Fungi Proteobacteria Eubacteria:
MetazoaEuglenozoa
Actinobacteria
Spirochaetes
Viridiplantae Acidobacteria
MycetozoaFungi
Bacteroidetes
Thermotogales
Eubacteria:BacteroidetesViridiplantae
MetazoaFirmicutes
Thermus
Actinobacteria
PlanctomycetesEubacteria:
Mycetozoa
Proteobacteria Bacteroidetes
ProteobacteriaAcidobacteria
Rhodophyta
Spirochaetes Archaea:
Archaea:Actinobacteria
Viridiplantae
Crenarchaeota
EuryarchaeotaBacteroidetes
Eubacteria:
FibrobacteresActinobacteria
FirmicutesBacteroidetes
ProteobacteriaCyanobacteriaFirmicutesProteobacteriaSpirochaetesThermotogales
Archaea:CrenarchaeotaEuryarchaeota
COG3345 COG3345 None
Origin
KOG2366 None None
Knownenzymaticactivities
EC 3.2.1.22 EC 3.2.1.22 EC 3.2.1.49 EC 3.2.1.20
COG/KOG
Firmicutes
Actinobacteria
ActinobacteriaDeinococcus
Acidobacteria
Thermus
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(β/α)8-barrel-type retaining α-D-glycopyranosidase families
GH66?
α-glucosidasesuperfamily
clan GH-H
GH13
GH70
GH77
COG0296
COG0366
COG1523
COG3280
COG1649
α-galactosidasesuperfamily
clan GH-D
GH27
GH36
GH36A
GH36B
GH36C
GH36D
GH31
family II
family III
GH38
GH57?
GH97
GH27a
GH27b
GH27c
GH97c
GH97d
GH97e
GH97a
GH97b ?
?
?
??
?
– [EC 3.2.1.22]
– [EC 3.2.1.49]
– [EC 3.2.1.20]
– ORF?
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Rigden DJ. Iterative database searches demonstrate that glycoside hydrolase families 27, 31, 36,and 66 share a common evolutionary origin with family 13. FEBS Lett. 2002, 523(1-3):17-22.
clans
GH-D
GH-H
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Nagano N, Porter CT, Thornton JM. The (β/α)8 glycosidases: sequence and structureanalyses suggest distant evolutionary relationships. Protein Eng. 2001, 14(11):845-855.
clans: GH-H GH-A GH-K?
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GH14 GH44 GH71
GH17 GH26 GH30 GH35 GH39
GH42 GH50 GH51 GH53 GH59 GH72 GH79 GH86
clan GH-AGH29
type I
GH1 GH2 GH5 GH10
GH67 GH89
type IV
GH13GH36 GH70GH31
COG1649
GH27
GH36A GH36B GH36C GH36D
GH77
clan GH-D clan GH-H
type II
type III
GH66 GH97
GH84
GH20
GH85GH25
GH18
clan GH-K
(β/α)8-barrel fold
GH56GH3
α-galactosidasesuperfamily
GH6 GH38 GH57
(β/α)7-barrel fold
TIM-barrelfold type
A hierarchical classification of the(β/α)8-type glycosyl hydrolases
α-glucosidasesuperfamily
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(β)3-solenoidinversion (axial orientation)28, 49GH-N(a/a)6inversion (equatorial orientation)8, 48GH-M(a/a)6inversion (axial orientation)15, 65GH-L(β/a)8 -barrelretention (equatorial orientation)18, 20GH-K5-fold β-propellerretention (β-furanoside)32, 68GH-Ja+βinversion (equatorial orientation)24, 46, 80GH-I(β/a)8 -barrelretention (axial orientation)13, 70, 77GH-HNot knowninversion (axial orientation)37, 63GH-G5-fold β-propellerinversion (equatorial orientation)43, 62GH-F6-fold β-propellerretention (equatorial orientation)33, 34, 83GH-E(β/a)8 -barrelretention (axial orientation)27, 36GH-Dβ-jelly rollretention (equatorial orientation)11, 12GH-Cβ-jelly rollretention (equatorial orientation)7, 16GH-B
(β/a)8 -barrelretention (equatorial orientation)1, 2, 5, 10, 17, 26, 30, 35, 39,42, 50, 51, 53, 59, 72, 79, 86
GH-A
Tertiary StructureOptical ConfigurationFamilies (GH)Clan
Clans of Glycoside HydrolasesClic
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COG2152NoneNoneCOG3507COG1621 / KOG0228COG / KOG
Eukaryota:FungiMetazoaViridiplantae
Eubacteria:ActinobacteriaAquificalesCyanobacteriaFirmicutesProteobacteriaThermotogales
Archaea:CrenarchaeotaEuryarchaeota
Eubacteria:ActinobacteriaFirmicutesProteobacteria
Archaea:Euryarchaeota
Eukaryota:Fungi
Eubacteria:ActinobacteriaProteobacteria
Eukaryota:FungiViridiplantae
Eubacteria:ActinobacteriaBacteroidetesFirmicutesProteobacteriaThermotogales
Eukaryota:EuglenozoaFungiParabasalideaViridiplantae
Eubacteria:ActinobacteriaBacteroidetesChloroflexiFirmicutesFusobacteriaProteobacteriaThermotogales
Archaea:Euryarchaeota
Origin
Not knownRetainingNot knownInvertingRetainingMolecularmechanism
Not knownEC 2.4.1.xEC 2.4.1.9EC 2.4.1.10EC 3.2.1.26
EC 3.2.1.55EC 3.2.1.8EC 3.2.1.37EC 3.2.1.55EC 3.2.1.99
EC 2.4.1.99EC 2.4.1.100EC 2.4.1.xEC 3.2.1.7EC 3.2.1.26EC 3.2.1.65EC 3.2.1.80
Knownenzymaticactivities
Not knownGH-JGH-FGH-FGH-JClan
GHLPGH68GH62GH43GH32Family
b-fructosidase (furanosidase) superfamilyClic
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A hierarchical structure of the b-fructosidase (furanosidase) superfamily
furanosidasesuperfamily
GH32
GH68
GH43
GH62
GHLP
clan GH-J
clan GH-F
GH32a
GH32b
GH32c
GH32d
GH68a
GH68b
GH43a
GH43b
GH43c
GH43d
GH43e
GH43f
GH43g
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(β)3-solenoidinversion (axial orientation)28, 49GH-N(a/a)6inversion (equatorial orientation)8, 48GH-M(a/a)6inversion (axial orientation)15, 65GH-L(β/a)8 -barrelretention (equatorial orientation)18, 20GH-K5-fold β-propellerretention (β-furanoside)32, 68GH-Ja+βinversion (equatorial orientation)24, 46, 80GH-I(β/a)8 -barrelretention (axial orientation)13, 70, 77GH-HNot knowninversion (axial orientation)37, 63GH-G5-fold β-propellerinversion (equatorial orientation)43, 62GH-F6-fold β-propellerretention (equatorial orientation)33, 34, 83GH-E(β/a)8 -barrelretention (axial orientation)27, 36GH-Dβ-jelly rollretention (equatorial orientation)11, 12GH-Cβ-jelly rollretention (equatorial orientation)7, 16GH-B
(β/a)8 -barrelretention (equatorial orientation)1, 2, 5, 10, 17, 26, 30, 35, 39,42, 50, 51, 53, 59, 72, 79, 86
GH-A
Tertiary StructureOptical ConfigurationFamilies (GH)Clan
Clans of Glycoside Hydrolases
Strohmeieret al.(2004)
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Thank you for the attention!
Please, visit my web-site to find a list of publications:http://bioinform.genetika.ru/members/Naumoff/index.htm
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