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CAZyme Information: MGYG000003019_00099

You are here: Home > Sequence: MGYG000003019_00099

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 Alistipes sp900553175
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900553175
CAZyme ID MGYG000003019_00099
CAZy Family GT35
CAZyme Description Maltodextrin phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
801 MGYG000003019_1|CGC4 89295.44 5.2147
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003019 1454145 MAG China Asia
Gene Location Start: 120784;  End: 123189  Strand: -

Full Sequence      Download help

MTNQISRDEL  RSAIADKLCA  HFGVTAGDAT  DEQVFQAAAI  VIREILSRLH  TFDSRTAPER60
EVHYLSMEFL  MGRSLMKDAF  NLGIGDALTG  ALEDLGRSAA  DIFETEPDAG  LGNGGLGRLA120
ACYMDSLATE  GIPATGYSLC  YELGIFRQRI  VDGRQTEVAD  NWRTAASSWL  VPCHEDTVEV180
RFGGRVEQHW  DAYGHYHGEL  RGYESVLAVP  RDMLIAPYGD  GRVNTLRLWE  AHSPNDLDMY240
LFAAGSYVQS  LEQRTMAEVI  TKVLYPADDH  MEGKTLRIRQ  QYFFVSATAQ  SILRAHRARY300
GTVRNFAEHH  VIQINDTHPT  LIIPELMRLL  LDDDGLGWDE  AWAIVTACVN  YTNHTVMSEA360
LETWPQGLIQ  SQLPRVWEII  CEINRRWCDE  LRARFGDDAR  VGRNLIIADG  SVHMANLCLA420
ACKTINGVSA  LHGEILRRDL  FRDVCALDPG  RFTYVTNGID  HRRWLAQCNP  GLHALVCDVL480
GSDRYLLHPE  ELAGLERAAD  DPAVLARLEE  IKALNKQRLA  AWVFRTDGFS  LNSDAILDVQ540
VKRLHEYKRQ  LLCAMRITQL  QLLLHDDPDQ  PFQPRTFLFA  AKAAPGYAVA  KRIIQLLCSL600
AADVNADPVC  RGRLQVYFLP  NYRVSAAEML  MPAAQVSEQI  STAGKEASGT  GNMKLMMNGA660
VTIGTLDGAN  VEMFEQLGAD  NMFLFGLHAD  EAEALRAAGY  DPQAYVRRSP  WLGRVLERMS720
CGYADGESYA  DLVSSLLYGG  DPYLLLADFD  DYAATHERLY  TTIADPAVRA  RLSLVNIARS780
GIFAADRAVR  EYAERIWEVH  A801

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Created with Snap408012016020024028032036040044048052056060064068072076091799GT35
Family Start End Evalue family coverage
GT35 91 799 5.7e-234 0.9970326409495549

CDD Domains      download full data without filtering help

Created with Snap40801201602002402803203604004404805205606006406807207605799PRK149862801GlgP21800PRK1498514799P_ylase11799GT35_Glycogen_Phosphorylase
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14986 PRK14986 0.0 5 799 12 810
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 2 801 1 750
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 21 800 20 797
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 14 799 1 794
glycogen/starch/alpha-glucan phosphorylases. This family consists of phosphorylases. Members use phosphate to break alpha 1,4 linkages between pairs of glucose residues at the end of long glucose polymers, releasing alpha-D-glucose 1-phosphate. The nomenclature convention is to preface the name according to the natural substrate, as in glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, etc. Name differences among these substrates reflect differences in patterns of branching with alpha 1,6 linkages. Members include allosterically regulated and unregulated forms. A related family, TIGR02094, contains examples known to act well on particularly small alpha 1,4 glucans, as may be found after import from exogenous sources. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
cd04300 GT35_Glycogen_Phosphorylase 0.0 11 799 1 795
glycogen phosphorylase and similar proteins. This is a family of oligosaccharide phosphorylases. It includes yeast and mammalian glycogen phosphorylases, plant starch/glucan phosphorylase, as well as the maltodextrin phosphorylases of bacteria. The members of this family catalyze the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism. The allosteric control mechanisms of yeast and mammalian members of this family are different from that of bacterial members. The members of this family belong to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.

CAZyme Hits      help

Created with Snap40801201602002402803203604004404805205606006406807207603799ANU40324.1|GT353799QQR06906.1|GT353799QIA32151.1|GT356799QUO35271.1|GT356799BCK80927.1|GT35
Hit ID E-Value Query Start Query End Hit Start Hit End
ANU40324.1 0.0 3 799 5 809
QQR06906.1 0.0 3 799 5 809
QIA32151.1 0.0 3 799 2 806
QUO35271.1 0.0 6 799 4 801
BCK80927.1 0.0 6 799 4 801

PDB Hits      download full data without filtering help

Created with Snap4080120160200240280320360400440480520560600640680720760217987TM7_A237992C4M_A297993ZCP_A297992GJ4_A297992FFR_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
7TM7_A 5.18e-211 21 798 29 801
ChainA, Alpha-1,4 glucan phosphorylase [Klebsiella pneumoniae subsp. pneumoniae HS11286],7TM7_B Chain B, Alpha-1,4 glucan phosphorylase [Klebsiella pneumoniae subsp. pneumoniae HS11286]
2C4M_A 1.44e-208 23 799 22 788
Starchphosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_B Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_C Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_D Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae]
3ZCP_A 6.40e-208 29 799 47 828
Rabbitmuscle glycogen phosphorylase b in complex with N- cyclohexancarbonyl-N-beta-D-glucopyranosyl urea determined at 1.83 A resolution [Oryctolagus cuniculus]
2GJ4_A 7.03e-208 29 799 35 816
Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2FFR_A 7.25e-208 29 799 35 816
Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]

Swiss-Prot Hits      download full data without filtering help

Created with Snap40801201602002402803203604004404805205606006406807207603799sp|Q9Z8N1|PHSG_CHLPN40799sp|Q9XTL9|PYG_DROME29799sp|P00489|PYGM_RABIT29799sp|P79334|PYGM_BOVIN29799sp|O18751|PYGM_SHEEP
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9Z8N1 2.64e-213 3 799 10 814
Glycogen phosphorylase OS=Chlamydia pneumoniae OX=83558 GN=glgP PE=3 SV=1
Q9XTL9 1.81e-207 40 799 64 828
Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
P00489 6.99e-207 29 799 47 828
Glycogen phosphorylase, muscle form OS=Oryctolagus cuniculus OX=9986 GN=PYGM PE=1 SV=3
P79334 1.35e-206 29 799 47 828
Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
O18751 1.91e-206 29 799 47 828
Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3

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
1.000035 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003019_00099.