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CAZyme Information: MGYG000000032_02754

You are here: Home > Sequence: MGYG000000032_02754

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 Hungatella effluvii
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Hungatella; Hungatella effluvii
CAZyme ID MGYG000000032_02754
CAZy Family GH2
CAZyme Description Exo-beta-D-glucosaminidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
822 MGYG000000032_6|CGC5 95787.13 4.8589
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000032 6969476 Isolate United Kingdom Europe
Gene Location Start: 195494;  End: 197962  Strand: +

Full Sequence      Download help

MKSYMELNEN  WSMRKSGDTK  WRPASIPGSV  YSNLLEQGEM  KNPYYGENQY  EVCEISRNDF60
EFACYFIVTE  DIIAQEKNFL  QFDGLDTLVD  IYLNGQKLGR  ADNMHRTWRY  DVTGAINTEL120
NELKLYFYSP  IRYIEEKQAE  RPLWGVATTI  PGYPYLRKAH  FMYGWDWGPQ  LPDMGIWRKV180
TLYGVSKALL  DNIHIRQEHK  SGGVELSIQA  EIEAFSEGRF  DMDVRILDPE  GKVIAICKKR240
LNGKDCNCEM  KINNPKLWWP  NGYGEQPLYT  VEARLMEGDC  CIDSKTVRTG  LRTIRVSRDD300
DQWGQEFCIV  VNETKIFAMG  ADYIPEDQII  SRCSPSKTRH  LLEQCVKANF  NHIRVWGGGC360
YPEDYFFDIC  DELGLLVWQD  FMFACAVYRM  SEDFTNNIRQ  EIIENVKRIR  NHASLALWCG420
NNEMETAWDS  WEIPQDQDLK  EDYLFQFEEL  IPEICRQYDP  DTFYWPSSPS  CGGNFEDPNS480
YTRGDVHYWD  VWHGMKPLTE  FRKFYFRFCS  EYGFMSLPNQ  KTINDFAAPE  ECNLFSAVME540
AHQKCDDGNK  KLLYYLSQMV  SYPYSFEGLI  YATQLLQADA  IRSNVEHMRR  NRGRCMGSTY600
WQVNDSNPII  SWSSIDYNGR  WKALHYYAKR  FYAPVLLSVN  EENLEEVVFN  ISNEQVTGIE660
GVICWTLRDA  GAHVLKEGKA  EVKAAPLSAK  DCFQLNLSKE  LDTIEKKRSH  YLEYAFYDST720
GQNRSYGTTL  FVMPKHFRFK  SPNITFCVTE  ETGGYRIQLK  AEAFAKGVCL  DLKKYDCSFS780
DNWFDIHGEE  TVSVWVGRDT  ISHAIDRNEL  EENLIIYCSN  DL822

Enzyme Prediction      help

No EC number prediction in MGYG000000032_02754.

CAZyme Signature Domains help

Created with Snap41821231642052462873283694114524935345756166576987397803712GH2
Family Start End Evalue family coverage
GH2 3 712 3.7e-101 0.7127659574468085

CDD Domains      download full data without filtering help

Created with Snap41821231642052462873283694114524935345756166576987397807638LacZ190292Glyco_hydro_2742821Ig_mannosidase76423ebgA175296PRK10150
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3250 LacZ 1.27e-100 7 638 15 635
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
pfam00703 Glyco_hydro_2 1.51e-13 190 292 3 106
Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
pfam17753 Ig_mannosidase 1.95e-11 742 821 2 78
Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.
PRK10340 ebgA 3.95e-11 76 423 126 449
cryptic beta-D-galactosidase subunit alpha; Reviewed
PRK10150 PRK10150 3.18e-10 175 296 169 280
beta-D-glucuronidase; Provisional

CAZyme Hits      help

Created with Snap41821231642052462873283694114524935345756166576987397805816CCO04426.1|GH25816AUG59052.1|GH25816QUH28340.1|GH27816ADU28568.1|GH25822AWB45455.1|GH2
Hit ID E-Value Query Start Query End Hit Start Hit End
CCO04426.1 1.65e-308 5 816 5 820
AUG59052.1 2.49e-297 5 816 3 811
QUH28340.1 9.17e-287 5 816 4 812
ADU28568.1 8.50e-285 7 816 6 812
AWB45455.1 2.15e-280 5 822 4 817

PDB Hits      download full data without filtering help

Created with Snap418212316420524628732836941145249353457561665769873978057862VJX_A57862JE8_A57867OP6_A57862WBK_A57862VQU_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VJX_A 3.35e-160 5 786 9 806
Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VJX_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VQT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VR4_A Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482],2VR4_B Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482]
2JE8_A 3.54e-160 5 786 11 808
Structureof a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JE8_B Structure of a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
7OP6_A 3.65e-160 5 786 11 808
ChainA, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP6_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_A Chain A, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482]
2WBK_A 9.62e-160 5 786 9 806
Structureof the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482],2WBK_B Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482]
2VQU_A 4.03e-158 5 786 9 806
Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQU_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron]

Swiss-Prot Hits      download full data without filtering help

Created with Snap41821231642052462873283694114524935345756166576987397803643sp|Q2TXB7|MANBB_ASPOR5784sp|Q29444|MANBA_BOVIN5784sp|Q95327|MANBA_CAPHI3643sp|B8NW36|MANBB_ASPFN7643sp|A1CGA8|MANBB_ASPCL
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q2TXB7 8.23e-103 3 643 5 664
Beta-mannosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=mndB PE=3 SV=3
Q29444 3.36e-102 5 784 23 844
Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1
Q95327 9.06e-102 5 784 23 844
Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1
B8NW36 2.27e-101 3 643 5 664
Beta-mannosidase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=mndB PE=3 SV=1
A1CGA8 3.24e-101 7 643 9 664
Beta-mannosidase B OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=mndB PE=3 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
1.000041 0.000007 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000032_02754.