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CAZyme Information: MGYG000002365_01709

You are here: Home > Sequence: MGYG000002365_01709

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Bifidobacterium globosum
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium globosum
CAZyme ID MGYG000002365_01709
CAZy Family GH36
CAZyme Description Alpha-galactosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
745 MGYG000002365_1|CGC29 81832.26 5.3849
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002365 2036949 Isolate Kenya Africa
Gene Location Start: 1982487;  End: 1984724  Strand: -

Full Sequence      Download help

MAIMDFHGTS  SRGEEVRIVY  FEQRAARSAF  ALAIVGDELP  RIVHWGRPLA  DPRTLVAAAD60
ALRPQRVSGT  LDETAWPSIL  PTQAEAWIGS  PRFVVRAGGM  ELFCRFAVTD  VRIDDDGVTV120
DARDAEQGVR  ILWRCELRES  GLVRQRMTVV  NMRSGELEIG  TVELAFPVPA  DMTEILTTTG180
HHLRERSSQR  QPFTIGRFQK  ASLVGRPDFD  SSLLLNVGRT  GFGFTHGEVY  SVHVAWSGNS240
LMAAERLPYT  SGLIGGAEAL  SGGEVTLCVQ  GGAGGDGACY  TTPWLYGAYG  EGLNEVAARF300
HTELRTTHTQ  WRAELGVPEK  PRPVILNTWE  AVYFQHDFGT  LKALADKAAA  SGVERFVVDD360
GWFGGRRDDT  AGLGDWWVSQ  DVWPDGDHSL  KALADYVHAK  GMEFGLWFEP  EMVNPDSAMY420
REHPDWVLRP  TANRLPMQGR  NQQVVDLTNP  QAYEYVYGCM  DALVTELGID  YIKWDHNKYV480
TEAVSPRTGR  PAVHGQTLAV  YRIFHDLKTA  HPGLEIESCS  SGGGRVDLAI  LSLADRIWAS540
DCVDPVERAD  IQRYTSLLVP  PEMIGEHVGA  SPAHSTHRAT  SQQMRMAMAF  FGHLGIEWNL600
LKEPQSALDE  LGVWVDAYKR  HRADFAHGTV  IHGDEADPAV  RVDGVVSASG  ERAVYRFTQL660
TTSQTYPAAP  VRLLGLDPDA  DYLIQPLACN  IGSGEPFTQI  GNGQSELGWW  NSQGIVMNGG720
ALAAFGLRPP  CIHPANAVLF  SATRV745

Enzyme Prediction      help

EC 3.2.1.22

CAZyme Signature Domains help

Created with Snap377411114918622326029833537240944748452155859663367070726687GH36
Family Start End Evalue family coverage
GH36 26 687 6.6e-210 0.9665697674418605

CDD Domains      download full data without filtering help

Created with Snap3774111149186223260298335372409447484521558596633670707280628Melibiase321620GH3642685GalA39263Glyco_hydro_36N352406GH27
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam02065 Melibiase 6.40e-159 280 628 2 347
Melibiase. Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.
cd14791 GH36 9.08e-112 321 620 1 299
glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
COG3345 GalA 1.83e-108 42 685 23 649
Alpha-galactosidase [Carbohydrate transport and metabolism].
pfam16875 Glyco_hydro_36N 9.72e-38 39 263 2 252
Glycosyl hydrolase family 36 N-terminal domain. This domain is found at the N-terminus of many family 36 glycoside hydrolases. It has a beta-supersandwich fold.
cd14792 GH27 1.06e-09 352 406 36 84
glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.

CAZyme Hits      help

Created with Snap37741111491862232602983353724094474845215585966336707071745AIZ16935.1|GH361745ASW24133.1|GH361745ATO39429.1|GH361745ABB76662.1|GH36|3.2.1.223745ATU19939.1|GH36
Hit ID E-Value Query Start Query End Hit Start Hit End
AIZ16935.1 0.0 1 745 1 745
ASW24133.1 0.0 1 745 1 745
ATO39429.1 0.0 1 745 1 745
ABB76662.1 0.0 1 745 1 741
ATU19939.1 0.0 3 745 4 746

PDB Hits      download full data without filtering help

Created with Snap3774111149186223260298335372409447484521558596633670707216874FNQ_A1746843MI6_A1846874FNR_A1746822XN0_A1746822XN2_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
4FNQ_A 2.06e-74 21 687 12 695
Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
3MI6_A 3.82e-74 174 684 192 695
ChainA, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_B Chain B, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_C Chain C, Alpha-galactosidase [Levilactobacillus brevis ATCC 367],3MI6_D Chain D, Alpha-galactosidase [Levilactobacillus brevis ATCC 367]
4FNR_A 7.10e-72 184 687 201 695
Crystalstructure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_B Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_C Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_D Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
2XN0_A 1.98e-71 174 682 195 693
Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN0_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN1_A Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_C Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_D Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM]
2XN2_A 3.78e-71 174 682 195 693
Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM]

Swiss-Prot Hits      download full data without filtering help

Created with Snap377411114918622326029833537240944748452155859663367070768744sp|P16551|RAFA_ECOLX184687sp|Q9ALJ4|AGAA_GEOSE174682sp|G1UB44|MELA_LACAC166684sp|P27756|AGAL_STRMU137683sp|G4T4R7|AGASK_RUMGN
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P16551 2.42e-112 68 744 49 706
Alpha-galactosidase OS=Escherichia coli OX=562 GN=rafA PE=1 SV=1
Q9ALJ4 3.89e-71 184 687 201 695
Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA PE=1 SV=1
G1UB44 1.08e-70 174 682 195 693
Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1
P27756 2.31e-70 166 684 177 684
Alpha-galactosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=aga PE=3 SV=3
G4T4R7 7.12e-69 137 683 153 683
Bifunctional alpha-galactosidase/sucrose kinase AgaSK OS=Ruminococcus gnavus OX=33038 GN=agaSK PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000062 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002365_01709.