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CAZyme Information: MGYG000001332_01311

You are here: Home > Sequence: MGYG000001332_01311

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 Massilioclostridium methylpentosum
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Massilioclostridium; Massilioclostridium methylpentosum
CAZyme ID MGYG000001332_01311
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1673 MGYG000001332_12|CGC1 184957.18 4.2677
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001332 3406391 Isolate not provided not provided
Gene Location Start: 61713;  End: 66734  Strand: +

Full Sequence      Download help

MKQKRMNFSR  MGKTLVAALL  SAALLLPTVG  TAVQASDILS  SQTETVQVIR  PYITGMETVG60
TELKGMYTYY  DVNGRPEAGS  SFRWLRCDTK  LGVYTEIPGA  TGSNYTLTPE  DAGKYIRFEV120
TPRTSDEAGS  AQQSWMIGPV  LTAEQYERID  NRFDNDNDFM  ANVNSIQSDI  ASRLANAVYF180
TVDSEGLHGS  EVFYKNNVQG  DFDPSTKPVV  QDGTVYAPAA  FFTLLLDAEA  PDVEATTIDG240
ATYYNLKQAA  AVLDKQMWSG  DEQQSEIANF  QMEHLGQGLI  VLSDTEAIFD  PVTDRDLIDE300
ACNMLYTLRA  TEEQMQWFRD  AKYGMFLHWD  PSSQIGVEIS  WDRKAFRPAD  IGSSYYNAID360
PEYDTLGQTF  NPTEYNPDEW  MQLAKEAGMK  YVVLTTKHHA  SYSNFFSDYD  NHTIKETPYN420
QDIVEKYVAA  AKKAGLKVGF  YYSARDWYNP  NYLTADHHRY  LEYYFGQIQE  LMTNYGDIDV480
MWFDSIGTSS  LNQWDPRTLL  RRMKQINPDV  IVNNRYTAVL  AGYDKSPYDV  NGDWYTPEHR540
LGGFDSSRPW  ESCMTVTEAP  GGGWSYRPNG  RVKSVEESVK  YLINNVVNDG  NLLYNIGPMP600
NGKLNETHAD  VFRQVGKWLE  PYKEAIYNTR  GGPYQNPQWG  GSTYRTDENG  LETIYLHVTP660
LLKGYTPSGN  SLQIDAPGNG  QTYSSASLVK  DGKEVQLTYN  EDGILLTLPE  GESWDAYDTV720
IRLTPDIAAT  LASKISQAQS  YADSLTSELL  ATVRQIVENQ  VAEAKQVLDS  GETSRYTEQL780
GLLNNCVQYA  RSAEALADAV  VSAEQKMESV  AVGTNPWECP  QYLYDSLQNN  ISAAKSLLDA840
ADSTAAQFDK  SASALNTAVE  SLNDLMNSLV  ITFTPDQGRV  DNGTTFSMSQ  SWQELNIRYT900
LDGSEPDVSS  AIYQGEQLTI  PAGIMTVKAA  LFDANGKKVG  ATCKHTYLNT  ENVQNLSPLA960
SSVQASSIYS  ESYTGAKACD  GNMNTRWATP  DGTITATLEL  QFDSPQTVNT  AQIQEYLDSG1020
ETTRISKFAI  EYWQDGGWKQ  AYTGDKVGAN  KVFSFAEFTS  DRVRLNIESC  MNVTIWEFSL1080
FQLEDSVGVT  ADKTNLRPNE  TAQLAVSGQL  ADGKPITPEM  IEDVTYHTDR  DDLVSIDETG1140
KLRIKEFSDE  ISFAVWADVT  FNGKTVTTEK  LSFKASVLGE  NLALGKTASA  SSVYGGGFEA1200
PKAVDGNDRT  RWASKVSSSY  WFEVDFGKEE  QVNNIAFQVY  SDRSDPVNYE  VYTDFKIQYL1260
KDGTWMDAYD  SSSMTHQITY  PVYNGTESYN  NVWIDSSGTV  KSTDYLVSFD  TVTASKIRLF1320
SDNTKKDPSI  IEFGAYYVPE  QAIVDKSGLD  AAIQQAAEYE  GKESEYTADS  WAALCTALET1380
ANTVFDDPDA  DQETVDAAAT  ALQEAIDGLV  KREPVETNKT  ILKKVLDYAV  QAKAGEEYAN1440
VIASVKASFD  AALLAADRVY  QDAAASQAEV  DRAWMDLLSE  IHKLGFQAGD  KTQLELLLSY1500
AKTIDLTNYV  QQGQAEYTAA  LAAAQVCFED  GDALTNEVNL  AAQQLLDAMM  NLRLKADKSI1560
LEELLVRSGR  IDTTLYSAET  IDSFLQAKKE  AERVFADSES  TQQAVDSAAD  NLERALERLL1620
PLEAPAIQGH  QGNSTSANGS  PKTGDPFSVA  CILLLAASGS  VLLKKKQRPD  SNK1673

Enzyme Prediction      help

No EC number prediction in MGYG000001332_01311.

CAZyme Signature Domains help

Created with Snap8316725033441850158566975283692010031087117112541338142215051589308628GH2911871321CBM32
Family Start End Evalue family coverage
GH29 308 628 3.3e-90 0.8988439306358381
CBM32 1187 1321 7.8e-16 0.8145161290322581

CDD Domains      download full data without filtering help

Created with Snap8316725033441850158566975283692010031087117112541338142215051589315677Alpha_L_fucos315624Alpha_L_fucos354630AfuC11871271F5_F8_type_C9621076F5_F8_type_C
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00812 Alpha_L_fucos 3.38e-80 315 677 20 384
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.
pfam01120 Alpha_L_fucos 4.29e-78 315 624 19 333
Alpha-L-fucosidase.
COG3669 AfuC 1.59e-27 354 630 33 323
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam00754 F5_F8_type_C 3.05e-12 1187 1271 1 83
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam00754 F5_F8_type_C 1.48e-09 962 1076 1 121
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.

CAZyme Hits      help

Created with Snap831672503344185015856697528369201003108711711254133814221505158945723QWP43961.1|GH2945723QWP00755.1|GH2945723QHV13030.1|GH2945723QHV15492.1|GH2945723QHV69491.1|GH29
Hit ID E-Value Query Start Query End Hit Start Hit End
QWP43961.1 1.27e-217 45 723 17 699
QWP00755.1 1.27e-217 45 723 17 699
QHV13030.1 7.18e-217 45 723 28 710
QHV15492.1 7.18e-217 45 723 28 710
QHV69491.1 1.01e-216 45 723 28 710

PDB Hits      download full data without filtering help

Created with Snap83167250334418501585669752836920100310871171125413381422150515893077246GN6_A3097014JL2_A3097014PCS_A3097012WVS_A3097012WVT_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
6GN6_A 2.62e-62 307 724 23 442
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]
4JL2_A 5.23e-42 309 701 13 415
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 5.64e-42 309 701 13 415
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]
2WVS_A 6.12e-42 309 701 17 419
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]
2WVT_A 6.12e-42 309 701 17 419
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 Snap8316725033441850158566975283692010031087117112541338142215051589317710sp|Q5RFI5|FUCO2_PONAB317710sp|Q9BTY2|FUCO2_HUMAN317709sp|Q6AYS4|FUCO2_RAT317710sp|Q99LJ1|FUCO_MOUSE317655sp|Q99KR8|FUCO2_MOUSE
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q5RFI5 2.14e-34 317 710 47 445
Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 SV=1
Q9BTY2 1.32e-33 317 710 49 447
Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2
Q6AYS4 5.10e-33 317 709 41 438
Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1
Q99LJ1 3.63e-32 317 710 38 432
Tissue alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca1 PE=1 SV=1
Q99KR8 1.37e-31 317 655 43 390
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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000335 0.998861 0.000209 0.000209 0.000184 0.000164

TMHMM  Annotations      download full data without filtering help

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