CAZyme Information: MGYG000004382_02131

Basic Information

• Species: UBA2821 sp902763335
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA2821; UBA2821 sp902763335
• CAZyme ID: MGYG000004382_02131
• CAZy Family: GT35
• CAZyme Description: Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
783		89600.84	5.3153

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004382	2786990	MAG	Israel	Asia

• Gene Location: Start: 10947; End: 13298 Strand: +

Full Sequence      

MSTFKENIVTILDLDYNKTIKEASTVELYNAVSKAAMKSIANQWSWETDRKKVCYLSAEF
LVGRLIYNNLLSLGLMNQLTELFSENGIDIGIFEDIEDNALGNGGLGRLAACFLDSAATQ
NIVVNGYGIRYRYGIFKQYFENGFQKETADDWTRFGDPWSVRREEDKVKINFKGQSVWAV
PYDTPVIGYGAGMINTLRLWQAEPIEEFNFELFNEQKYDKSVKEKNDAEAITSVLYPNDS
TDAGKKLRLKQQYFFSSASLQDIIKKYKAKYGNDFSHLGDEYAVQLNDTHPVVSIPELCR
ILVEEEGVTFAKALKICKEVFAYTNHTVMAEALEKWSVKLFKSVIPNVYKYVVKINNALL
KDLDKLGISDEEKKNYQIIDTPYGNDWVVIQMARLAIYASHSTNGVAQIHTEILKADTLK
EWYKIYPERFNNKTNGITQRRWLALANMELAGFINDKIGNEWITNLDKLKDLEKYADDKE
VIKKFDEIKKIKKKQLADYIKAKENIDVNPEFIFDVQVKRLHEYKRQLLNAFSILDTYYG
IKDGRIKDFTPTVYIFGAKSAPGYLRAKGIIKYINEISKMIANDPEVKDKMQVVFVSNYC
VSYAEKIVPAADFSEQISTAGTEASGTSNMKFMLNGAVTLGTYDGANIEIVEQAGEENNY
IFGAKVEEIEKIKDTYDAKKMYNENPRIKKVVDTLVDGTFSDDGTGLFKELFDSLLEGAS
WHAPDQYYLFLDFESYCDTRLRANQDFKNTAEFRRKCFMNTANAGKFSSDRTIIDYAKEI
WNA

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	86	782	7.9e-254	0.9896142433234422

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	41	782	60	809	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	2	783	7	748	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	48	783	56	796	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	16	782	9	793	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	5	782	1	794	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
BCN32947.1	0.0	2	781	6	779
BCJ96995.1	0.0	2	782	3	778
BCJ92464.1	0.0	4	781	5	777
CUH92218.1	0.0	4	782	5	778
QEY34129.1	0.0	1	781	1	776

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C4M_A	3.31e-238	23	781	28	786	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	5.21e-217	43	781	76	829	Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]
5OX0_A	1.07e-215	1	781	25	826	GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]
2GJ4_A	1.65e-215	1	781	13	814	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2FFR_A	1.70e-215	1	781	13	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
Q9XTL9	1.16e-220	27	781	51	826	Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
P79334	2.22e-217	1	781	25	826	Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
O18751	1.26e-216	1	781	25	826	Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
P11216	2.59e-216	43	781	73	826	Glycogen phosphorylase, brain form OS=Homo sapiens OX=9606 GN=PYGB PE=1 SV=5
Q5R5M6	1.04e-215	43	781	73	826	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
1.000054	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004382_02131.