CAZyme Information: MGYG000003072_02998

Basic Information

• Species: Paenibacillus amylolyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus amylolyticus
• CAZyme ID: MGYG000003072_02998
• CAZy Family: GT35
• CAZyme Description: Glycogen phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
810	MGYG000003072_11|CGC4	92533.44	5.2579

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003072	7042795	MAG	China	Asia

• Gene Location: Start: 163631; End: 166063 Strand: -

Full Sequence      

MFDNKETFKSIFTRNLVSKLGKPIEEATQEDVYHVLGSMIREYAGQDWATSNQGFKQRQD
KQVYYFSLEFLIGRLLGNNLLNVNELELVRDSLAELGFSLEEIEEQEADAGLGNGGLGRL
AACFLDSLASLRYAGHGCGIRYKYGLFEQKIINGNQVELPDNWLDKGNEWEVRRPDKKVE
VQFWGRVEAHEQDGEYQFVTKDAESVVAIPYDVPVIGYGQTHVNTLRLWSAEPKRETSLD
TPSNYYGYLDYSRSVESISEFLYPDDSQYEGKLLRLKQQYFMCSAGVQSALRTFNKLELP
YDRLPDKVAFHINDTHPTLVIPELMRILIDVKGYGWDEAWDITTRTVSYTNHTTLSEALE
KWPVSMISRLLPRIYMIIEEINKRFCGMLLDRYPGDQDRIGHLAIVANDQVRMAHLAIVG
SHSVNGVAALHTEILKEREMAPFYELYPERFNNKTNGITHRRWLMHANPKLSDLITDTIG
NEWITEPGKLDQLAGFADNTSFQEQFRSIKRDNKERLATYILDHTGTAMNPDSIFDVQVK
RLHGYKRQLLNILHVMHLYNRLKNDASFDMVPRTFIFGAKAAPSYYFAKKIIKLINNVAD
TVNRDAAVNDRLKVFFLENYSVSLAEKIIPAADVSEQISTAGKEASGTGNMKFMMNGALT
IGTMDGANVEMAEQVGEENMFIYGLRADEVLEYYRSGSYRPNEIVQHDERIREVVEQLVH
PGAFCYRDGEFWDIYDSLLAHGDEYFVLRDFAAYADAHAAIDQAYRDIPGWTRKAILNTA
HSGIFSSDRTISEYATDIWGIHPVSGNWKG

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	93	801	6.9e-281	0.9955489614243324

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	8	804	23	813	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	4	803	5	750	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	61	799	59	794	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	12	801	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	12	801	4	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
APO45477.1	0.0	1	810	1	810
QZN73827.1	0.0	1	810	1	810
QOS78625.1	0.0	1	810	1	810
QLG41112.1	0.0	1	810	1	810
QKS54864.1	0.0	1	810	1	810

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5IKO_A	1.52e-256	3	803	27	833	Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]
2GJ4_A	7.60e-254	3	803	11	818	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A	7.86e-254	3	803	11	818	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	9.29e-254	3	803	16	823	ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]
2FFR_A	1.11e-253	3	803	11	818	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
P39123	0.0	1	804	1	797	Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
Q5MIB6	5.31e-256	3	803	24	830	Glycogen phosphorylase, brain form OS=Ovis aries OX=9940 GN=PYGB PE=2 SV=3
P11216	7.51e-256	3	803	24	830	Glycogen phosphorylase, brain form OS=Homo sapiens OX=9606 GN=PYGB PE=1 SV=5
Q3B7M9	8.56e-255	3	803	24	830	Glycogen phosphorylase, brain form OS=Bos taurus OX=9913 GN=PYGB PE=2 SV=3
Q5R5M6	1.72e-254	3	803	24	830	Glycogen phosphorylase, brain form OS=Pongo abelii OX=9601 GN=PYGB 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
1.000043	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003072_02998.