CAZyme Information: MGYG000000389_00134

Basic Information

• Species: Roseburia sp900550935
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; Roseburia sp900550935
• CAZyme ID: MGYG000000389_00134
• CAZy Family: GT35
• CAZyme Description: Glycogen phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
750		85568.86	5.0918

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000389	2762523	MAG	Sweden	Europe

• Gene Location: Start: 151656; End: 153908 Strand: -

Full Sequence      

MNLQEIVTKRCGKSIADCSNEELYYSLLEMTKGMAKEKESNAGKRKLYYISAEFLIGKLL
SNNLINLGIYEDVKKLLAENGKSLAEVEEVEPEPSLGNGGLGRLAACFLDSIASLGLNGD
GVGLNYHYGLFKQVFENNLQHETPNPWIEKESWLTKTDVTYPISFGGFTLQSRLYDIDVI
GYENRTTKLHLFDVETVDESLVGNGIDFNKEDIAKNLTLFLYPDDSDDKGRILRVYQQYF
MVSNAARLIIDETLARGGDLHKLNEYVVIQINDTHPSMVIPEMIRLLMERGILMDEAIDI
VSKTCAYTNHTILAEALEKWPIHFLEKAVPQLLPIIYELNSRVTKKYDDKSVAIIDDENR
VHMAHMDIHYGYSVNGVAYLHTEILKNTELNNFYKIYPEKFNNKTNGITFRRWLLHCNSE
LADLFTSLIGDGYKKNAEELEKLGKYVDDPAVLQKLLDVKSARKADLKAYLEKTQGIVLD
DNSIYDIQIKRLHEYKRQQMNALYVIHKYFEIKAGKKPARPITVIFGAKAAPAYVIAKDI
IHLILCLQEVISKDPEVSPYLKVVMVENYNVTLAEKLIPAADIHEQISLASKEASGTSNM
KFMLNGAIAIGTMDGANVEMHQFVGDDNIYIFGESSEAVIEHYEKADYVSRSYYENDADI
KRAIDFIVSDTLMAVGCRENLERLYNELLNKDWFMTLPDFKDYVATKERIYADYEDRMAW
AKKMLINISKAGFFSSDRTIAQYNEDIWHL

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	77	750	4.3e-230	0.9955489614243324

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	45	750	70	810	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	2	750	12	748	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	40	748	54	794	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	10	750	8	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	2	750	3	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL08110.1	0.0	1	750	14	763
CBL12671.1	0.0	1	750	14	763
VCV23296.1	0.0	1	750	23	772
AEN95921.1	0.0	1	750	1	750
ADF57356.1	0.0	1	723	1	723

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4L22_A	0.0	7	749	12	756	Crystalstructure of putative glycogen phosphorylase from Streptococcus mutans [Streptococcus mutans UA159]
2C4M_A	1.13e-178	36	750	51	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]
2FFR_A	3.20e-170	45	748	69	814	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
5OX0_A	1.07e-169	45	748	81	826	GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]
2GJ4_A	1.73e-169	45	748	69	814	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P29849	0.0	1	750	2	751	Maltodextrin phosphorylase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malP PE=3 SV=2
P39123	1.05e-188	11	750	20	794	Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
P79334	6.54e-171	45	748	81	826	Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
O18751	6.54e-171	45	748	81	826	Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
Q9XTL9	1.09e-169	45	748	81	826	Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000028	0.000011	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000389_00134.