CAZyme Information: MGYG000003762_01071

Basic Information

• Species: Corynebacterium aurimucosum_C
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium; Corynebacterium aurimucosum_C
• CAZyme ID: MGYG000003762_01071
• CAZy Family: GT35
• CAZyme Description: Glycogen phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
634		72112.27	4.5018

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003762	2238677	MAG	Canada	North America

• Gene Location: Start: 3821; End: 5725 Strand: -

Full Sequence      

MENGYDFIIRRASEQRLVHFDDMDVRAIPYDMPITGYGTDNVGTLRLWKSEPIDEFDYDA
FNSQRFTEAIVERERVMDICRVLYPNDTTYEGKVLRVRQQYFFVSASLQQMIDNYIEHHG
EDLTGFAEYNCIQLNDTHPVLAIPELLRLLLDEHGMGWDDAWKVVTETFAYTNHTVLAEA
LESWEVSIFQKLFWRIWELVEEIDRRFREDMAQRGLDQGRIDYMAPVSDGHVHMAWIACY
AAYSINGVAALHTEIIKADTLSEWHELWPEKFNNKTNGVTPRRWLRMCNPRLSDLLTEQA
GSDAWVTDLTELAKLAPLAEDEKVLRQLINIKRANKQDFAAWIDAHQGASVDPDSIFDVQ
IKRLHEYKRQLMNALYILDLYFRIKVDGETVPKRTFIFGAKAAPGYVRAKAIIKLINAIG
DLVNNDPATKDVLNVVFVENYNVSPAEHIIPAADVSEQISVAGKEASGTSNMKFMMNGAL
TLGTMDGANVEIVEAVGEENAYIFGARNEEIPQLRAEYNPGELYNTVPGLARVLDAFTDG
TLGSENAGMFGDLRSSLLDGFGEHAQDTYYVLGDFADYRETRDRMAADYDADELAWAKKA
WLNICYSGRFSSDRTIADYANEVWKLAPTPIANV

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	3	626	6.8e-218	0.887240356083086

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	24	628	210	812	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	24	628	175	750	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	25	625	200	795	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	2	626	154	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	1	626	156	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
ACP33204.1	0.0	1	634	163	796
QQU92667.1	0.0	1	634	163	796
QQU94609.1	0.0	1	634	163	796
QPS59238.1	0.0	1	634	163	796
QQA79973.1	0.0	1	634	163	796

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C4M_A	0.0	2	630	164	792	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	4.49e-179	21	629	206	819	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
2GJ4_A	6.15e-179	21	629	206	819	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A	6.34e-179	21	629	206	819	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	7.36e-179	21	629	211	824	ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P73511	7.91e-183	25	631	228	831	Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1
P79334	5.12e-179	21	629	218	831	Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
O18751	2.88e-178	21	629	218	831	Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
P00489	5.92e-178	21	629	218	831	Glycogen phosphorylase, muscle form OS=Oryctolagus cuniculus OX=9986 GN=PYGM PE=1 SV=3
P11217	8.11e-178	21	629	218	831	Glycogen phosphorylase, muscle form OS=Homo sapiens OX=9606 GN=PYGM PE=1 SV=6

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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003762_01071.