logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001159_00249

You are here: Home > Sequence: MGYG000001159_00249

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 pullorum
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium pullorum
CAZyme ID MGYG000001159_00249
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
438 MGYG000001159_12|CGC1 50296.4 5.1184
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001159 2232439 MAG Austria Europe
Gene Location Start: 118799;  End: 120115  Strand: -

Full Sequence      Download help

MTLFVFDRDA  YERRMTWYRH  ARFGMFLHWG  LYAIPARGEW  IRSVEQMPEE  PYRRYFEEFN60
PVDFDARRWA  RAAKEAGMQY  VVLTAKHHDG  FCLFDSQYTD  WKSTNTPFGR  DIVREFVDAV120
RAEGLRVGLY  YSLLDWHHPD  YPHRHDANHP  DRNNESVSDE  GRDFDRYLDY  MHAQVRELCT180
NYGKIDVLWF  DFSYDNLRGE  AWRGTELMRM  VRSLQPDVIV  DNRLEVSGEG  YGSLAAGEPT240
PYHGDFVSPE  QMIPPNGIQD  VHGNDLAWEA  CVTMNGSWGY  TADDHAFKPA  PMLIRKLVEC300
VSKGGNMLLN  VGPDARGRFP  KQSVEILSQI  GAWMDENHDS  IYGCGRSDLP  KPEYGRITAN360
AETKTLYFHV  YENSIGALPL  IGVRKEQIDS  IRYLASGAEV  PISTSWTHSD  YPDIVFADLG420
ADPVLPDPVD  TVLAVKLR438

Enzyme Prediction      help

EC 3.2.1.51

CAZyme Signature Domains help

Created with Snap2143658710913115317519721924026228430632835037239441611343GH29
Family Start End Evalue family coverage
GH29 11 343 5.3e-117 0.8901734104046243

CDD Domains      download full data without filtering help

Created with Snap2143658710913115317519721924026228430632835037239441617337Alpha_L_fucos12370Alpha_L_fucos28343AfuC65191GHL670223GH36
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01120 Alpha_L_fucos 9.56e-116 17 337 21 331
Alpha-L-fucosidase.
smart00812 Alpha_L_fucos 4.71e-115 12 370 17 370
Alpha-L-fucosidase. O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis.
COG3669 AfuC 3.93e-47 28 343 1 321
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam14871 GHL6 2.89e-07 65 191 1 134
Hypothetical glycosyl hydrolase 6. GHL6 is a family of hypothetical glycoside hydrolases.
cd14791 GH36 1.44e-06 70 223 25 197
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.

CAZyme Hits      help

Created with Snap214365871091311531751972192402622843063283503723944163438BAQ31854.1|GH293438QOV18680.1|GH293438QQQ91833.1|GH293438ANU78473.1|GH293438ASU31287.1|GH29
Hit ID E-Value Query Start Query End Hit Start Hit End
BAQ31854.1 2.70e-294 3 438 1 434
QOV18680.1 1.15e-249 3 438 1 434
QQQ91833.1 9.38e-249 3 438 1 434
ANU78473.1 9.38e-249 3 438 1 434
ASU31287.1 9.38e-249 3 438 1 434

PDB Hits      download full data without filtering help

Created with Snap21436587109131153175197219240262284306328350372394416104386GN6_A154112WVS_A154114JL2_A154114PCS_A154112WVT_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
6GN6_A 6.21e-183 10 438 26 444
Alpha-L-fucosidaseisoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_B Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_C Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_D Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_E Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_F Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus]
2WVS_A 2.39e-70 15 411 23 420
Crystalstructure of an alpha-L-fucosidase GH29 trapped covalent intermediate from Bacteroides thetaiotaomicron in complex with 2- fluoro-fucosyl fluoride using an E288Q mutant [Bacteroides thetaiotaomicron VPI-5482],2WVS_B Crystal structure of an alpha-L-fucosidase GH29 trapped covalent intermediate from Bacteroides thetaiotaomicron in complex with 2- fluoro-fucosyl fluoride using an E288Q mutant [Bacteroides thetaiotaomicron VPI-5482],2WVS_C Crystal structure of an alpha-L-fucosidase GH29 trapped covalent intermediate from Bacteroides thetaiotaomicron in complex with 2- fluoro-fucosyl fluoride using an E288Q mutant [Bacteroides thetaiotaomicron VPI-5482],2WVS_D Crystal structure of an alpha-L-fucosidase GH29 trapped covalent intermediate from Bacteroides thetaiotaomicron in complex with 2- fluoro-fucosyl fluoride using an E288Q mutant [Bacteroides thetaiotaomicron VPI-5482]
4JL2_A 5.67e-70 15 411 19 416
Crystalstructure of a bacterial fucosidase with a monovalent iminocyclitol inhibitor [Bacteroides thetaiotaomicron VPI-5482],4JL2_B Crystal structure of a bacterial fucosidase with a monovalent iminocyclitol inhibitor [Bacteroides thetaiotaomicron VPI-5482]
4PCS_A 5.99e-70 15 411 19 416
Crystalstructure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCS_B Crystal structure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCS_C Crystal structure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCS_D Crystal structure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_A Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_B Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_C Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_D Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482]
2WVT_A 6.65e-70 15 411 23 420
Crystalstructure of an alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron in complex with a novel iminosugar fucosidase inhibitor [Bacteroides thetaiotaomicron VPI-5482],2WVT_B Crystal structure of an alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron in complex with a novel iminosugar fucosidase inhibitor [Bacteroides thetaiotaomicron VPI-5482],2WVU_A Crystal structure of a Michaelis complex of alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron with the synthetic substrate 4- nitrophenyl-alpha-L-fucose [Bacteroides thetaiotaomicron VPI-5482],2WVU_B Crystal structure of a Michaelis complex of alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron with the synthetic substrate 4- nitrophenyl-alpha-L-fucose [Bacteroides thetaiotaomicron VPI-5482],2WVU_C Crystal structure of a Michaelis complex of alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron with the synthetic substrate 4- nitrophenyl-alpha-L-fucose [Bacteroides thetaiotaomicron VPI-5482],2WVU_D Crystal structure of a Michaelis complex of alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron with the synthetic substrate 4- nitrophenyl-alpha-L-fucose [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits      download full data without filtering help

Created with Snap2143658710913115317519721924026228430632835037239441617372sp|P10901|FUCO_DICDI16342sp|Q9BTY2|FUCO2_HUMAN16342sp|Q5RFI5|FUCO2_PONAB9367sp|Q6AYS4|FUCO2_RAT9367sp|Q99KR8|FUCO2_MOUSE
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P10901 4.31e-42 17 372 36 392
Alpha-L-fucosidase OS=Dictyostelium discoideum OX=44689 GN=alfA PE=3 SV=1
Q9BTY2 4.43e-39 16 342 48 368
Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2
Q5RFI5 2.16e-38 16 342 46 366
Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 SV=1
Q6AYS4 6.86e-37 9 367 31 388
Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1
Q99KR8 1.35e-36 9 367 33 390
Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 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
1.000040 0.000005 0.000001 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001159_00249.