logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002127_00547

You are here: Home > Sequence: MGYG000002127_00547

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
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Butyricicoccaceae; Agathobaculum;
CAZyme ID MGYG000002127_00547
CAZy Family GT35
CAZyme Description Glycogen phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
756 85197.4 5.2172
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002127 1040318 MAG Mongolia Asia
Gene Location Start: 37;  End: 2307  Strand: -

Full Sequence      Download help

MPKTQYTKTA  LKQAIAGKLQ  RHFACEVADA  TKDQVYEACA  LVVRDALTEH  MIETQNEVER60
DGERQVHYLC  MEFLVGRSLR  NNAYNLGILD  ALTAALKDMG  FEMADIFEEE  ADPGLGNGGL120
GRLAACYMDG  MATDGVRGTG  YSIRYEHGIF  KQKIVEGQQV  ELPDSWLATG  EVWQIPAMDE180
TREVKIGGTV  DTYFDDNGKL  VVNYHDYTPV  LAVPYDMPIS  GYDTNNIARL  RLWKAQSPIA240
LDMKLFSSGE  YLKALEKHAL  AETISMVLYP  EDNHREGQSL  RLKQQYFLVS  ATLQDICAKH300
KVKYGTLENF  AHKHVLHIND  THPTLVIPEL  MRILMDENDM  SWEQAWNITS  QSVAYTNHTV360
MPEALECWPV  SLMQELMPRI  MQIIYEINER  FCKELWNYFP  NDFQKISKLA  IVADDTVRMA420
HLAIAGSFSI  NGVSALHSEI  LKERVFTDFY  NIYSSKFCNV  TNGIAHRRWL  CEANPELAEL480
IESKIGKGYR  THPSELQVLN  NYADDKELLD  KLGEIKRHNK  QRLADYIKAH  NGIEVNMDSI540
FDVQVKRLHE  YKRQMLNILH  IISLYHKLKD  NPDMDFVPRT  FIFGSKAAPG  YAVAKKTIQL600
INSISKMIDN  DPAVRDKLKV  VFLEDYKVSL  AEIIMPAAEV  SEQISIAGKE  ASGTGNMKFM660
MNGALTIGTM  DGANVEICEA  VGQENIFIFG  METPEAEALA  ASGNYEPMVI  YQNDPVIRRV720
LDQMIHGFGD  GVDYTDIANL  LLHGGNGGPA  DPKSPF756

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Created with Snap377511315118922626430234037841545349152956760464268071895742GT35
Family Start End Evalue family coverage
GT35 95 742 2.8e-247 0.9065281899109793

CDD Domains      download full data without filtering help

Created with Snap377511315118922626430234037841545349152956760464268071810727PRK1498610729GlgP2752PRK1498527745P_ylase12745GT35_Glycogen_Phosphorylase
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14986 PRK14986 0.0 10 727 16 730
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 10 729 8 668
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 2 752 1 739
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 27 745 13 735
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 12 745 1 736
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 Snap37751131511892262643023403784154534915295676046426807186744BCK80927.1|GT357751BCK78905.1|GT355751ANU40324.1|GT355751QQR06906.1|GT355751QIA32151.1|GT35
Hit ID E-Value Query Start Query End Hit Start Hit End
BCK80927.1 1.28e-303 6 744 3 737
BCK78905.1 2.39e-303 7 751 2 741
ANU40324.1 4.83e-301 5 751 6 751
QQR06906.1 4.83e-301 5 751 6 751
QIA32151.1 6.16e-301 5 751 3 748

PDB Hits      download full data without filtering help

Created with Snap3775113151189226264302340378415453491529567604642680718307432GJ4_A307432GM9_A307432FFR_A307437O8E_A307431ABB_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2GJ4_A 2.35e-227 30 743 35 756
Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A 2.43e-227 30 743 35 756
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]
2FFR_A 2.43e-227 30 743 35 756
Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
7O8E_A 2.86e-227 30 743 40 761
ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]
1ABB_A 3.79e-227 30 743 37 758
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 Snap377511315118922626430234037841545349152956760464268071829742sp|P39123|PHSG_BACSU30742sp|Q9XTL9|PYG_DROME30743sp|P79334|PYGM_BOVIN30743sp|O18751|PYGM_SHEEP3742sp|P73511|PHSG_SYNY3
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P39123 1.97e-235 29 742 26 732
Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
Q9XTL9 2.52e-234 30 742 47 767
Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
P79334 2.78e-230 30 743 47 768
Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
O18751 5.57e-230 30 743 47 768
Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
P73511 1.59e-228 3 742 21 765
Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 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
1.000062 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002127_00547.