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CAZyme Information: MGYG000000453_00266

You are here: Home > Sequence: MGYG000000453_00266

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 Eubacterium_R sp900539775
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp900539775
CAZyme ID MGYG000000453_00266
CAZy Family GH112
CAZyme Description 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
729 MGYG000000453_1|CGC5 84493.3 5.0164
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000453 1755797 MAG Sweden Europe
Gene Location Start: 316669;  End: 318858  Strand: -

Full Sequence      Download help

MDKKRGRVTI  PTDMDVVKET  IEIMDVWGAD  AIRDCDGTEF  PQELKNTGAK  IYATYYTTRK60
DNAWAKANPD  EIQQMYIMTS  FHTAVEEKLE  IHLMDHLYPD  MLAVNTRDDI  KRWWEVMDRT120
IGEPVPTDEW  SYDEKSGNVV  INPVKKFHEY  TVSFLAYIMW  DPVHMYNAVV  NEWNVEPQIT180
FDVRQPKTRA  HSLERLRRFL  DTHDYVDVVR  FTTFFHQFTL  IFDELAREKF  VDWFGYSASV240
SPYILKQFEE  EVGYKFRPEF  IIDQGYMNNT  YRIPSKEFRD  FQAFQRREVA  KLAKEMVDIV300
HEYGKEAMMF  MGDHWIGMEP  FMDDFASIGL  DAVVGSVGNG  ATLRLFSDIK  NVKYTEGRFL360
PYFFPDVFHE  GGDPIYEAKV  NWVTARRAIL  RSPIQRIGYG  GYLKLALKFP  EFVDYIKGVC420
DEFRTLYDNI  QGTTPYCVKK  VAVLNCWGKM  RAWSNHMVHH  GLYYRQNYSY  FGVIEALSGA480
PFDVSFISFD  DIKENKNFLN  QFDVVINVGD  ADTAQSGGEY  WCDEEIITAV  KEFVYNGGGF540
IGVGEPAAHQ  WQGKFFQLDD  ILGVERENGF  TLNTRRYNTQ  EHRDHFILAD  ANGEVDFGEG600
KKNIVALDGT  TVLIQNASEL  PFAVRHAEEV  QMAVKSFGKG  RGVYISGLPY  SFKNSRVLYR660
AVLWSSNSED  ELNKWFSTNY  NVEVHAYVKN  GKYCVVNNTY  EPQDTTVYTG  DGNGFDLHLE720
ANEIKWYQI729

Enzyme Prediction      help

EC 2.4.1.211 2.4.1.-

CAZyme Signature Domains help

Created with Snap36721091451822182552913283644004374735105465836196566926727GH112
Family Start End Evalue family coverage
GH112 6 727 0 0.9972027972027973

CDD Domains      download full data without filtering help

Created with Snap36721091451822182552913283644004374735105465836196566925728TIGR023366438Lact_bio_phlase440670LBP_M675727LBP_C
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02336 TIGR02336 0.0 5 728 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 6 438 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 1.11e-123 440 670 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 1.95e-25 675 727 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 Snap36721091451822182552913283644004374735105465836196566921729CBL18493.1|GH1121729QCU02958.1|GH1126729QHB23220.1|GH1126729QEI30710.1|GH1122729QRT29560.1|GH112
Hit ID E-Value Query Start Query End Hit Start Hit End
CBL18493.1 0.0 1 729 1 720
QCU02958.1 0.0 1 729 1 720
QHB23220.1 0.0 6 729 7 720
QEI30710.1 0.0 6 729 7 720
QRT29560.1 0.0 2 729 3 720

PDB Hits      download full data without filtering help

Created with Snap367210914518221825529132836440043747351054658361965669267263WFZ_A67262ZUS_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3WFZ_A 4.18e-223 6 726 5 748
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 9.52e-222 6 726 5 748
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 Snap36721091451822182552913283644004374735105465836196566926729sp|A9KIW5|GAHP2_LACP72727sp|A9KQ75|GAHP1_LACP76726sp|E8MF13|LNPA_BIFL25716sp|A9KHK4|GLRP_LACP7
Hit ID E-Value Query Start Query End Hit Start Hit End Description
A9KIW5 0.0 6 729 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 2 727 3 719
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 4.00e-221 6 726 5 748
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 4.80e-147 5 716 9 715
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
1.000034 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000453_00266.