logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000223_00100

You are here: Home > Sequence: MGYG000000223_00100

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 NSJ-61 sp003433845
Lineage Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; NSJ-61; NSJ-61 sp003433845
CAZyme ID MGYG000000223_00100
CAZy Family GH112
CAZyme Description 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
718 MGYG000000223_1|CGC4 83308.01 4.7803
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000223 4367631 Isolate China Asia
Gene Location Start: 114897;  End: 117053  Strand: +

Full Sequence      Download help

MKTKGRVTVP  TDVDVIDETL  RIIDLWGADA  IRDCDGTNMP  EELSKLDIKQ  YATYYTTRKD60
NAWATAHPEE  IQQMYLMSDP  TTATKTSLRI  PLMKHYYEKQ  LKVNTIDDIK  RWWEVIDRTT120
GEVFPVENWS  YDENTQEVIL  NDCVPFHAYT  VSFLAFVIWD  PVHMYNALTN  EWKGEEHQMT180
YDVRQPKTQA  YVIEKLKRWI  KEHPEVDVIR  FTTFFHQFTL  MFNDQAKEKF  VDWFGYSASV240
SPYILKQFEE  EVGYPFRPEY  IINQGYHNST  FCVPTKEYKD  FMQFQMREVA  KLVKKLVDIT300
HEAGKEAMMF  LGDHWIGTEP  FGPYFKDLGI  DAVVGSVGSG  TTLRLISDIP  GVRYTEGRFL360
PYFFPDVFCE  GGDPIKEAKE  NWVTARRAIL  RSPLDRIGYG  GYLKLALKFP  DFVDYITSVC420
DEFRELYEHV  HGATPYVMPF  KVTILNSWGK  VRSWGTHMVA  HALWYKEIYS  YSGILEALSG480
MPFDVQFISF  DDILNDEHVL  DGAGVIINAG  DAYTAYSGGE  YWDNPKIVAA  LRKFVYEGGG540
FIGVGDPSAY  QKEGHFYQLY  DVLGVDKELG  FSLSTDKYNW  NEQAHFLNEG  LHDPFFGEEI600
KNVFALDETI  VLKDNRHNIQ  FATNTYGKGR  SVYLSGLPFS  FENARLLYRC  LFYAAHEEEN660
MKKWYSENCN  VEVNVYPNTN  SYCVVNNTYE  PQSSTIYTDK  DSYQIDLEAN  EIRWFTID718

Enzyme Prediction      help

EC 2.4.1.211 2.4.1.-

CAZyme Signature Domains help

Created with Snap35711071431792152512873233593944304665025385746106466825715GH112
Family Start End Evalue family coverage
GH112 5 715 0 0.9972027972027973

CDD Domains      download full data without filtering help

Created with Snap35711071431792152512873233593944304665025385746106466824715TIGR023365437Lact_bio_phlase441659LBP_M664715LBP_C
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02336 TIGR02336 0.0 4 715 3 718
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 5 437 1 433
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 1.23e-125 441 659 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 1.26e-19 664 715 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 Snap35711071431792152512873233593944304665025385746106466821718QNM10889.1|GH1121717BCT45816.1|GH1124717QSI26761.1|GH1124717QQR27382.1|GH1124717ASU18840.1|GH112
Hit ID E-Value Query Start Query End Hit Start Hit End
QNM10889.1 0.0 1 718 1 718
BCT45816.1 0.0 1 717 1 719
QSI26761.1 0.0 4 717 5 719
QQR27382.1 0.0 4 717 5 719
ASU18840.1 0.0 4 717 5 719

PDB Hits      download full data without filtering help

Created with Snap357110714317921525128732335939443046650253857461064668217143WFZ_A17142ZUS_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3WFZ_A 8.59e-241 1 714 1 748
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 1.97e-239 1 714 1 748
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 Snap35711071431792152512873233593944304665025385746106466825717sp|A9KIW5|GAHP2_LACP72716sp|A9KQ75|GAHP1_LACP71714sp|E8MF13|LNPA_BIFL23709sp|A9KHK4|GLRP_LACP7
Hit ID E-Value Query Start Query End Hit Start Hit End Description
A9KIW5 0.0 5 717 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 2 716 4 720
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 8.24e-239 1 714 1 748
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 9.27e-154 3 709 8 713
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
1.000048 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000223_00100.