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CAZyme Information: MGYG000000262_00367

You are here: Home > Sequence: MGYG000000262_00367

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 Anaerobutyricum hallii
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerobutyricum; Anaerobutyricum hallii
CAZyme ID MGYG000000262_00367
CAZy Family GT35
CAZyme Description Glycogen phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
811 MGYG000000262_2|CGC2 94133.19 5.6815
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000262 3404550 Isolate China Asia
Gene Location Start: 96651;  End: 99086  Strand: -

Full Sequence      Download help

MIKKDTFDKE  KFKKELESNV  RMLFRRKLEE  ATPQQIYQAV  AYSVKDDIID  NWIETHKAYE60
KQDKKMVYYM  SMEFLMGRAL  GNNMINLLCY  DDVRETLEEL  GLDLNLIEDQ  EPDAALGNGG120
LGRLAACFLD  SLATLGYPAY  GCGIRYRYGM  FKQKIENGYQ  VEVPDNWLKY  GNPFEIKRDE180
YAVEVKFGGY  VDVEMHNGRQ  KFVQKGYQSV  RAVPYDMPIV  GYGNHIVNTL  RIWDAEAINN240
FNLDSFDKGE  YEKAVEQENL  ARTICEVLYP  NDNHMAGKEL  RLKQQYFFIS  ASVQRAIAKY300
KETHDDIRKF  HEKVTFQLND  THPTVAVAEL  MRILVDEEGL  EWDEAWEITR  KTCAYTNHTI360
MAEALEKWPI  ELFSRLLPRV  YQIVEEINRR  FVIEIQNKYP  GDQEKIRKMA  ILYDGQVRMA420
HLAIAGSYSV  NGVARLHTDI  LKKRELKDFY  EMMPEKFNNK  TNGITQRRFL  LHGNPLLASW480
VTDKIGDDWI  TNLDHLKHLK  VYVDDEKCQQ  EFMNIKYQNK  VRLAKYIKEH  NGIDVDPRSI540
FDCQVKRLHE  YKRQLMNILH  VMYLYNEIKA  HPDMDIVPRT  FIFGAKAAAG  YYTAKLTIKL600
INAVADKINN  DPSINGKIKV  VFIEDYRVSN  AELIFAAADV  SEQISTASKE  ASGTGNMKFM660
LNGALTLGTM  DGANVEIVEE  VGKENAFIFG  LSADQIMEYE  KNGNYNPRDV  YNNNQDVRQV720
LTQLVNGFYS  PENPELFRAL  YDALLEKDTY  FTLLDFDSYK  EAHNRIDAAY  RDEEHWARTA780
MLQTASAGKF  SSDRTIEEYA  KEMWHLEKVT  L811

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Created with Snap408112116220224328332436440544648652756760864868972977097807GT35
Family Start End Evalue family coverage
GT35 97 807 1.1e-286 0.9970326409495549

CDD Domains      download full data without filtering help

Created with Snap408112116220224328332436440544648652756760864868972977039811PRK149868808GlgP6804PRK1498518806P_ylase13806GT35_Glycogen_Phosphorylase
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14986 PRK14986 0.0 39 811 44 815
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 8 808 5 750
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 6 804 4 794
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 18 806 3 794
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 13 806 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 Snap40811211622022432833243644054464865275676086486897297701811SOB73595.1|GT3522811QUF81626.1|GT357811QJU19430.1|GT357811QRP38873.1|GT357811ASN96342.1|GT35
Hit ID E-Value Query Start Query End Hit Start Hit End
SOB73595.1 0.0 1 811 1 811
QUF81626.1 0.0 22 811 1 790
QJU19430.1 0.0 7 811 5 815
QRP38873.1 0.0 7 811 5 815
ASN96342.1 0.0 7 811 5 815

PDB Hits      download full data without filtering help

Created with Snap4081121162202243283324364405446486527567608648689729770318075OX0_A318072GJ4_A318072GM9_A318077O8E_A318071ABB_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
5OX0_A 5.57e-290 31 807 47 829
GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]
2GJ4_A 8.23e-290 31 807 35 817
Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A 8.52e-290 31 807 35 817
Structureof rabbit muscle glycogen phosphorylase in complex with thienopyrrole [Oryctolagus cuniculus],5MCB_A Glycogen phosphorylase in complex with chlorogenic acid. [Oryctolagus cuniculus],7ONF_A Chain A, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]
7O8E_A 1.01e-289 31 807 40 822
ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]
1ABB_A 1.34e-289 31 807 37 819
ControlOf Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_B Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_C Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_D Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus]

Swiss-Prot Hits      download full data without filtering help

Created with Snap408112116220224328332436440544648652756760864868972977031807sp|P79334|PYGM_BOVIN31807sp|P00489|PYGM_RABIT31807sp|O18751|PYGM_SHEEP31807sp|Q9WUB3|PYGM_MOUSE31807sp|P11217|PYGM_HUMAN
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P79334 5.92e-289 31 807 47 829
Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
P00489 8.68e-289 31 807 47 829
Glycogen phosphorylase, muscle form OS=Oryctolagus cuniculus OX=9986 GN=PYGM PE=1 SV=3
O18751 1.68e-288 31 807 47 829
Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
Q9WUB3 9.61e-288 31 807 47 829
Glycogen phosphorylase, muscle form OS=Mus musculus OX=10090 GN=Pygm PE=1 SV=3
P11217 9.61e-288 31 807 47 829
Glycogen phosphorylase, muscle form OS=Homo sapiens OX=9606 GN=PYGM PE=1 SV=6

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
1.000067 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000262_00367.