CAZyme Information: MGYG000004245_01851

Basic Information

• Species: SFEL01 sp004557245
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-138; SFEL01; SFEL01 sp004557245
• CAZyme ID: MGYG000004245_01851
• CAZy Family: GT35
• CAZyme Description: Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
786		90124.08	5.8965

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004245	1999050	MAG	United Kingdom	Europe

• Gene Location: Start: 7414; End: 9774 Strand: -

Full Sequence      

MMEAAMIIRRMEEELRSDYQIELVEASTPQIHKALSNAVMYAISDNWRKARREHEHVRRA
YYFSAEYLMGRMVFNNLYCLGILDQIRDLLRARGCDIASMEDIEDAALGNGGLGRLAACF
LDSAATHDLPLDGYGLRYKFGLFKQSFKNGYQCEKADDWQRYGDPWSRRRDDKTVEITFA
DQKVMAVPYDMPIVGYGTDNIGTLRLWQSEPLEEFDFNLFNEQEYDLAVREKNKVEDITR
VLYPNDSTYEGKRLRLKQQYFLSSASLQDIIRRYKRVRGNDLSNFAAHCAIQLNDTHPTV
SIPELVRLLMNEGMDFDAAFDITRKTFSYTNHTIMSEALEKWDYDLFMSVVPELADIISR
INEVQNSELRARGVSQEQIDRMQIATGGQIHMARLAVFASTYVNGVAQIHSDILRHDLFK
DWYSVTPDKFQNKTNGITQRRWLGLCNRELSEFITERIGGGFITDLSEISKLKQHMSDAD
IAAFNAVKQQKKAQLSAVIREKEGVHIPPEFVFDVQVKRMHEYKRQLLNALSIMDIYYSL
KEGSLTDFTPTAFIFGAKAAPGYIRAKSIIKYINEVANLINSDPDMKDKLRVVFVQNYNC
SYAEHIMPAADISEQISPAGTEASGTGNMKFMLNGTVTLGTYDGANIEIAQEAGEENNYI
FGARVEELNAIRDTYNPREIYDREPRVKRVMDTLVNGTVSDGGTGKFAEIYNSILNGESW
HRPDNYFLLKDFMPYMEAKLRANHDYRDRIAFGRKCLMNTASAGKFSSDRTIAEYARELW
HIDSVK

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	91	782	4.4e-254	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	37	786	43	814	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	9	783	11	749	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	38	780	37	794	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	11	782	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	6	782	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
QCT06755.1	0.0	7	782	3	784
CBL34863.1	0.0	15	786	20	794
CBL34093.1	0.0	18	785	17	786
CBK96326.1	0.0	15	786	20	794
CBK95778.1	0.0	19	785	18	786

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C4M_A	1.95e-269	35	783	37	789	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	1.95e-223	34	783	58	832	Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]
2FFR_A	5.77e-220	34	783	43	817	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
1Z8D_A	1.41e-219	34	783	55	829	ChainA, Glycogen phosphorylase, muscle form [Homo sapiens]
5OX0_A	1.45e-219	34	783	55	829	GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q3B7M9	5.90e-227	26	780	47	826	Glycogen phosphorylase, brain form OS=Bos taurus OX=9913 GN=PYGB PE=2 SV=3
Q9XTL9	3.45e-226	34	783	55	829	Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
Q8CI94	2.68e-225	34	783	55	829	Glycogen phosphorylase, brain form OS=Mus musculus OX=10090 GN=Pygb PE=1 SV=3
P53534	6.45e-225	34	783	55	829	Glycogen phosphorylase, brain form (Fragment) OS=Rattus norvegicus OX=10116 GN=Pygb PE=1 SV=3
P11216	9.71e-223	34	783	55	829	Glycogen phosphorylase, brain form OS=Homo sapiens OX=9606 GN=PYGB PE=1 SV=5

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
1.000095	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004245_01851.