CAZyme Information: MGYG000003550_00984

Basic Information

• Species: Clostridium sp900769625
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900769625
• CAZyme ID: MGYG000003550_00984
• CAZy Family: GT35
• CAZyme Description: Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
752	MGYG000003550_31|CGC2	86288.61	4.8938

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003550	3104477	MAG	Fiji	Oceania

• Gene Location: Start: 41522; End: 43780 Strand: +

Full Sequence      

MLKKNLEQILDKKFEKTISTATNAEIYSALLQLTKTEEKEKGNNKGKKKLYYISAEFLIG
KLLSNNLINLGLYDEVKKVLAENGKDLTAIEEMELEPSLGNGGLGRLAACFLDSIATLGL
NGDGVGLNYHFGLFQQVFENNKQKAVKNPWLTDESWLNKSDIKFEVPFGGFKVTSTLYDI
DVTGYDKPCNKLRLFDIDTVDESLVTDGIDFDKTDIEKNLTLFLYPDDSDDAGRILRVYQ
QYFMVSNAAQLILLEAEENGYDLHKLHEHVAVQINDTHPSMVIPELIRLLGQKGIGMDEA
IEIVTKTCAYTNHTILAEALEKWPIDYLEKAVPQLMPIIRELDNKVKAKYDDEKVYIIDD
QRRVHMANMDIHYGYSVNGVAALHTEILKDVELKPFFDIYPEKFNNKTNGITFRRWLLHC
NNELADFITELIGDGYKKNADKLEELAKFVDDKNVLNKLDKIKKNNKIALKKYLKETQNL
DLNENSIFDIQIKRLHEYKRQQMNVLYIINKYLEIKSGKIPTTPITMIFGAKAAPAYVIA
QDIIHTILCLQEIIDKDPEVNKYLNVFMVENYNVTKASKLIPACDVSEQISLASKEASGT
GNMKFMLNGALTLGTEDGANVEIHQLVGDDNIYIFGESSEEVIEHYKNEDYVAKEYYEKE
NIKKLVDFITSDEMLRVGDKENLTRLHDELINKDWFMTLLDIEDYIKTKDRVFKDYEDRE
AWNKKVLINISKAGFFSSDRTIAQYNEDIWHL

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	80	752	4.5e-221	0.9955489614243324

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	50	752	72	810	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	2	752	9	748	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	52	750	63	794	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	16	752	11	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	3	752	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
QUF83643.1	0.0	1	752	1	752
BBK75267.1	0.0	1	752	1	752
QMW92473.1	0.0	1	752	1	752
ALS15614.1	0.0	1	752	1	752
APF22959.1	0.0	1	752	1	752

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4L22_A	0.0	4	751	6	756	Crystalstructure of putative glycogen phosphorylase from Streptococcus mutans [Streptococcus mutans UA159]
2C4M_A	1.00e-167	51	752	63	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]
5OX0_A	2.69e-164	2	750	28	826	GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]
2GJ4_A	4.37e-164	2	750	16	814	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2FFR_A	4.50e-164	2	750	16	814	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P29849	0.0	5	752	3	751	Maltodextrin phosphorylase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malP PE=3 SV=2
Q9XTL9	2.30e-169	2	750	28	826	Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
P39123	2.36e-169	37	752	50	794	Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
P79334	5.88e-166	2	750	28	826	Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
O18751	5.88e-166	2	750	28	826	Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3

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
1.000051	0.000005	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003550_00984.