CAZyme Information: MGYG000002008_00651

Basic Information

• Species: CAG-115 sp003516865
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; CAG-115; CAG-115 sp003516865
• CAZyme ID: MGYG000002008_00651
• CAZy Family: GT35
• CAZyme Description: Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
786	MGYG000002008_4|CGC1	88710.66	4.9668

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002008	2115917	MAG	Spain	Europe

• Gene Location: Start: 29341; End: 31701 Strand: +

Full Sequence      

MIDKTLLKNDFEDILRDSAANGKRRSPAQLHDALSKAIMRQAVPMMNCSAPDGRRAGYLS
MEFLVGRAIYNNILCLGLTDYAEELLNEAGGSLSELEEIEDAALGNGGLGRLAACFLDSA
ATLKLPLTGYGIRYKYGLFKQTIEDGFQREYADDWTKFGDPWSRRAEDETVIVHFADGDV
KAVPYDMPIFGYKNDFACTLRLWQAEPINAFDFDAFNRQDYFGAARGEIEAENISKTLYP
NDDARPGKLLRLRQEYFFSAASVEDMIRKHLEAGRPLSNFGEFNAIQLNDTHPVIAIPEL
IRNLINRGCSFEEALETAKKTFNYTNHTIMAEALEKWSCDIVEELVPEVYAIILRINEEF
ISDMYRRGIKREKIASMQLVAGGMVHMARMAIYCSSHVNGVARIHTEILKNDALHDWYEL
YPERFLNETNGITPRRWLALCNPKLADMITELLGNEKWLTDLTQLKNLRPFCDDKAIRDR
FSAIKQANKAALAEYIAIHEGEDIDPTSLFDIQIKRLHEYKRQLLNAFSILYIYFGIKDG
SISLGNFAPTTFIFGAKSAPGYARAKAIIKYINEIANLVNNDLSLNGAIKVVFVQNYNVS
YAEKLVVAADISEQISTAGTEASGTGNMKFMLNGTMTLGTYDGANVEIAEEAGEENNYIF
GARVEDLEKIMPEYDPRKLYSENTRIARVLNTLIDGTFTDGGNGSFRELYYSLLDGASWH
KPDHYYVLGDLENYVQAKLKANADYKFNHDEFVKKSMINMCFAGKFSSDRTISGYAEDIW
KISPDK

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	86	782	3.4e-247	0.9955489614243324

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	52	784	68	812	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	51	784	59	750	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	26	781	30	795	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	26	782	17	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	8	782	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBK96326.1	0.0	2	784	7	792
CBL34863.1	0.0	2	784	7	792
CCO05339.1	0.0	12	786	12	792
CBL18239.1	0.0	10	784	5	781
ADU23251.1	0.0	13	782	13	787

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C4M_A	2.93e-253	54	784	60	790	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]
5IKO_A	3.40e-207	52	784	82	833	Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]
1Z8D_A	1.69e-206	52	786	79	832	ChainA, Glycogen phosphorylase, muscle form [Homo sapiens]
2FFR_A	1.98e-206	52	786	67	820	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
5OX0_A	3.48e-206	52	786	79	832	GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P73511	2.82e-212	30	784	61	828	Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1
P79334	4.12e-207	52	786	79	832	Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
Q9Z8N1	4.67e-207	26	782	37	814	Glycogen phosphorylase OS=Chlamydia pneumoniae OX=83558 GN=glgP PE=3 SV=1
O18751	1.16e-206	52	786	79	832	Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
P11217	1.16e-206	52	786	79	832	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
1.000047	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002008_00651.