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CAZyme Information: MGYG000003291_00163

You are here: Home > Sequence: MGYG000003291_00163

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 Faecalibacterium prausnitzii_M
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium prausnitzii_M
CAZyme ID MGYG000003291_00163
CAZy Family GH112
CAZyme Description 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
720 MGYG000003291_26|CGC1 83169.66 5.1352
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003291 2081808 MAG Mongolia Asia
Gene Location Start: 3686;  End: 5848  Strand: +

Full Sequence      Download help

MDEMRKTGRV  TIPTDLDVVP  ETLEILKKWG  ADAIRDCDGT  DFPQQLKDVD  AKIYSTYYTT60
RKDNVWAKAN  PDEVQQCYIM  TGFYTAPGDT  VTIPLMKGIS  PELMQVNTND  DITRWWEVMD120
RTTGQPVPPE  RWSYVDGSVT  VQAVPFHEYT  VSFLAYLIWD  PVHMYNATTN  GWTNFEHQIT180
FDVRQPKTHK  YSMERLRKFI  AEHPYVNVIR  YTTFFHQFTL  IFDELKREKF  VDWYGYSASV240
SPCILNQFEQ  EVGYKFRPEY  IIDQGYYNNQ  YRVPSKEFRD  FQAFQRREVA  KLAKEMVDIT300
HECGCEAMMF  LGDHWIGTEP  FMPEFKTIGL  DAVVGSVGNG  STLRLISDIE  GVKYTEGRFL360
PYFFPDTFHE  GGDPVREAKE  NWVTARRAIL  RKPIDRIGYG  GYLKLALDFP  EFVDYVESVC420
NEFRQLYENI  KGTTPYCVKR  VAVLNCWGKM  RAWGCHMVHH  ALYYKQNYSY  AGVIEMLSGA480
PFDVRFISFE  DIKNNPALLD  ELDVIINVGD  ADTAHTGGIW  WEDPEITSAI  RKFVWNGGGF540
IGVGEPSGHA  YQGHLLQLAT  VLGVEEENGF  TLNYDKYNWT  EHPDHFILQD  ADQPVDFGEG600
KKNIYALEGT  QVLVQRNKEV  QMAAHDFGKG  RAVYISGVPY  SFANSRTLYR  AILWSAHSEE660
ELHTWFSSNY  NVEVHAYVKN  GKYCVVNNTY  QPEDTTVYTT  HGNHFDLHLD  ANEIKWYEIG720
720

Enzyme Prediction      help

EC 2.4.1.211 2.4.1.-

CAZyme Signature Domains help

Created with Snap36721081441802162522883243603964324685045405766126486848718GH112
Family Start End Evalue family coverage
GH112 8 718 0 0.9986013986013986

CDD Domains      download full data without filtering help

Created with Snap36721081441802162522883243603964324685045405766126486847718TIGR023368438Lact_bio_phlase440660LBP_M665717LBP_C
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02336 TIGR02336 0.0 7 718 3 719
1,3-beta-galactosyl-N-acetylhexosamine phosphorylase. Members of this family are found in phylogenetically diverse bacteria, including Clostridium perfringens (in the Firmicutes), Bifidobacterium longum and Propionibacterium acnes (in the Actinobacteria), and Vibrio vulnificus (in the Proteobacteria), most of which occur as mammalian pathogens or commensals. The nominal activity, 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase (EC 2.4.1.211), varies somewhat from instance to instance in relative rates for closely related substrates. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
pfam09508 Lact_bio_phlase 0.0 8 438 1 434
Lacto-N-biose phosphorylase N-terminal TIM barrel domain. The gene which codes for this protein in gut-bacteria is located in a novel putative operon for galactose metabolism. The protein appears to be a carbohydrate-processing phosphorolytic enzyme (EC:2.4.1.211), unlike either glycoside hydrolases or glycoside lyase. Intestinal colonisation by bifidobacteria is important for human health, especially in pediatrics, because colonisation seems to prevent infection by some pathogenic bacteria that cause diarrhoea or other illnesses. The operon seems to be involved in intestinal colonisation by bifidobacteria mediated by metabolism of mucin sugars. In addition, it may also resolve the question of the nature of the bifidus factor in human milk as the lacto-N-biose structure found in milk oligosaccharides.
pfam17385 LBP_M 1.21e-135 440 660 1 221
Lacto-N-biose phosphorylase central domain. The gene which codes for this protein in gut-bacteria is located in a novel putative operon for galactose metabolism. The protein appears to be a carbohydrate-processing phosphorolytic enzyme (EC:2.4.1.211), unlike either glycoside hydrolases or glycoside lyase. Intestinal colonisation by bifidobacteria is important for human health, especially in pediatrics, because colonisation seems to prevent infection by some pathogenic bacteria that cause diarrhoea or other illnesses. The operon seems to be involved in intestinal colonisation by bifidobacteria mediated by metabolism of mucin sugars. In addition, it may also resolve the question of the nature of the bifidus factor in human milk as the lacto-N-biose structure found in milk oligosaccharides.
pfam17386 LBP_C 2.12e-22 665 717 1 53
Lacto-N-biose phosphorylase C-terminal domain. The gene which codes for this protein in gut-bacteria is located in a novel putative operon for galactose metabolism. The protein appears to be a carbohydrate-processing phosphorolytic enzyme (EC:2.4.1.211), unlike either glycoside hydrolases or glycoside lyase. Intestinal colonisation by bifidobacteria is important for human health, especially in pediatrics, because colonisation seems to prevent infection by some pathogenic bacteria that cause diarrhoea or other illnesses. The operon seems to be involved in intestinal colonisation by bifidobacteria mediated by metabolism of mucin sugars. In addition, it may also resolve the question of the nature of the bifidus factor in human milk as the lacto-N-biose structure found in milk oligosaccharides.

CAZyme Hits      help

Created with Snap36721081441802162522883243603964324685045405766126486841719CBL02866.1|GH1121719AXA82973.1|GH1121719AXB28366.1|GH1121719CBK99351.1|GH1121719ATO99299.1|GH112
Hit ID E-Value Query Start Query End Hit Start Hit End
CBL02866.1 0.0 1 719 1 719
AXA82973.1 0.0 1 719 1 719
AXB28366.1 0.0 1 719 1 719
CBK99351.1 0.0 1 719 1 719
ATO99299.1 0.0 1 719 1 719

PDB Hits      download full data without filtering help

Created with Snap367210814418021625228832436039643246850454057661264868447183WFZ_A47182ZUS_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3WFZ_A 8.64e-231 4 718 1 750
Crystalstructure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant [Bifidobacterium longum subsp. longum JCM 1217],3WFZ_B Crystal structure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant [Bifidobacterium longum subsp. longum JCM 1217],3WFZ_C Crystal structure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant [Bifidobacterium longum subsp. longum JCM 1217],3WFZ_D Crystal structure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant [Bifidobacterium longum subsp. longum JCM 1217]
2ZUS_A 1.98e-229 4 718 1 750
Crystalstructure of Galacto-N-biose/Lacto-N-biose I phosphorylase [Bifidobacterium longum],2ZUS_B Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase [Bifidobacterium longum],2ZUS_C Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase [Bifidobacterium longum],2ZUS_D Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase [Bifidobacterium longum],2ZUT_A Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc [Bifidobacterium longum],2ZUT_B Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc [Bifidobacterium longum],2ZUT_C Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc [Bifidobacterium longum],2ZUT_D Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc [Bifidobacterium longum],2ZUU_A Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc [Bifidobacterium longum],2ZUU_B Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc [Bifidobacterium longum],2ZUU_C Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc [Bifidobacterium longum],2ZUU_D Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc [Bifidobacterium longum],2ZUV_A Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc, Ethylene glycol, and nitrate [Bifidobacterium longum],2ZUV_B Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc, Ethylene glycol, and nitrate [Bifidobacterium longum],2ZUW_A Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc and sulfate [Bifidobacterium longum],2ZUW_B Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc and sulfate [Bifidobacterium longum],2ZUW_C Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc and sulfate [Bifidobacterium longum],2ZUW_D Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc and sulfate [Bifidobacterium longum]

Swiss-Prot Hits      download full data without filtering help

Created with Snap36721081441802162522883243603964324685045405766126486848719sp|A9KIW5|GAHP2_LACP77717sp|A9KQ75|GAHP1_LACP74718sp|E8MF13|LNPA_BIFL28697sp|A9KHK4|GLRP_LACP7
Hit ID E-Value Query Start Query End Hit Start Hit End Description
A9KIW5 0.0 8 719 9 723
1,3-beta-galactosyl-N-acetylhexosamine phosphorylase Cphy0577 OS=Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) OX=357809 GN=Cphy_0577 PE=1 SV=1
A9KQ75 0.0 7 717 6 719
1,3-beta-galactosyl-N-acetylhexosamine phosphorylase Cphy3030 OS=Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) OX=357809 GN=Cphy_3030 PE=1 SV=1
E8MF13 8.28e-229 4 718 1 750
1,3-beta-galactosyl-N-acetylhexosamine phosphorylase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=lnpA PE=1 SV=1
A9KHK4 5.34e-150 8 697 10 700
D-galactosyl-beta-1->4-L-rhamnose phosphorylase OS=Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) OX=357809 GN=Cphy_1920 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
1.000061 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003291_00163.