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CAZyme Information: MGYG000000312_00060

You are here: Home > Sequence: MGYG000000312_00060

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 Eisenbergiella sp900539715
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900539715
CAZyme ID MGYG000000312_00060
CAZy Family GT35
CAZyme Description Glycogen phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
828 95583.94 5.712
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000312 2782709 MAG Sweden Europe
Gene Location Start: 59843;  End: 62329  Strand: -

Full Sequence      Download help

MLKKAPMKFD  KELFKGSVIN  NIKTLYRRTL  EEATPQQVFQ  AVSYAIKDVI  VDNWMISQKE60
YEKKDPKMVY  YMSMEFLMGR  ALGNNLINLC  AYSEVQEALD  ELGLDLNLIE  DQEPDPALGN120
GGLGRLAACF  LDSLATLNYA  AYGCGIRYRY  GMFRQEIQNG  FQVEVPDNWL  ADGYPFELRR180
PEYAKEVKFG  GWVSSYTDEN  GRTIFKQEGY  QSVKAVPYDM  PIVGYGNGIV  NTLRIWDAEP240
VECFSLDSFD  KGDYQKAVEQ  ENLARNIVEV  LYPNDNHYAG  KELRLKQQYF  FISASVQEAV300
EKYMRTHKDL  HKFHEKVAFQ  LNDTHPTVAV  AELMRVLMDD  YYLSWEEAWD  ITTKTCAYTN360
HTIMSEALEK  WPIELFSRLL  PRIYQIVEEI  NRRFVLQIQQ  MYPGNQEKIR  KMAIIYDGQV420
KMAHLAIVGG  HSVNGVARLH  TEILKNQELK  DFYEMMPAKF  NNKTNGITQR  RFLLHANPLL480
ADWVTDHVGD  EWITDLPAIS  KLRIYADDEK  AQQEFMNIKY  RNKVRLAKYI  REHNGIEIDP540
RSIFDVQVKR  LHEYKRQLMN  ILHIMYLYNQ  IKDHPDMEFY  PRTFIFGAKA  AAGYRNAKLT600
IKLINNVADV  INNDPVVNGR  IKVVFIENYR  VSNAEWIFAA  ADVSEQISTA  SKEASGTGNM660
KFMLNGALTL  GTMDGANVEI  VEEVGKENAF  IFGLSADQVI  QYENFGGYNP  MDIFNNDQDI720
RRVLMQLING  TYSANDTELF  RPLYNSLLNT  QSTSKADTYF  ILADFKAYAE  AQRRVEEAYR780
DEKNWAKSAI  LNVASAGKFS  SDRTIEEYVN  DIWHLDKVIL  PQKLEKTK828

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Created with Snap418212416520724828933137241445549653857962166270374578698815GT35
Family Start End Evalue family coverage
GT35 98 815 6.6e-282 0.9970326409495549

CDD Domains      download full data without filtering help

Created with Snap418212416520724828933137241445549653857962166270374578633820PRK1498610817GlgP8813PRK1498518815P_ylase15815GT35_Glycogen_Phosphorylase
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14986 PRK14986 0.0 33 820 36 815
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 10 817 5 750
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 8 813 4 794
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 18 815 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 15 815 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 Snap41821241652072482893313724144554965385796216627037457869820QNM02962.1|GT359820QBE95906.1|GT359820QIB55899.1|GT359820QMW76233.1|GT359820ASM70669.1|GT35
Hit ID E-Value Query Start Query End Hit Start Hit End
QNM02962.1 0.0 9 820 17 833
QBE95906.1 0.0 9 820 6 818
QIB55899.1 0.0 9 820 6 818
QMW76233.1 0.0 9 820 6 818
ASM70669.1 0.0 9 820 6 818

PDB Hits      download full data without filtering help

Created with Snap4182124165207248289331372414455496538579621662703745786338165OX0_A338162GJ4_A338162GM9_A338167O8E_A338161ABB_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
5OX0_A 1.04e-276 33 816 47 829
GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]
2GJ4_A 1.09e-276 33 816 35 817
Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A 1.13e-276 33 816 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 1.34e-276 33 816 40 822
ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]
1ABB_A 1.77e-276 33 816 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 Snap418212416520724828933137241445549653857962166270374578612820sp|P73511|PHSG_SYNY333816sp|P79334|PYGM_BOVIN33816sp|O18751|PYGM_SHEEP33816sp|P00489|PYGM_RABIT33816sp|Q9WUB3|PYGM_MOUSE
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P73511 2.04e-280 12 820 27 831
Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1
P79334 1.20e-277 33 816 47 829
Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
O18751 3.40e-277 33 816 47 829
Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
P00489 1.14e-275 33 816 47 829
Glycogen phosphorylase, muscle form OS=Oryctolagus cuniculus OX=9986 GN=PYGM PE=1 SV=3
Q9WUB3 6.30e-275 33 816 47 829
Glycogen phosphorylase, muscle form OS=Mus musculus OX=10090 GN=Pygm PE=1 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
1.000040 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000312_00060.