CAZyme Information: MGYG000003731_00285

Basic Information

• Species: Prevotella amnii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella amnii
• CAZyme ID: MGYG000003731_00285
• CAZy Family: GT35
• CAZyme Description: Glycogen phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
852		98298.24	6.6089

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003731	1790835	MAG	Canada	North America

• Gene Location: Start: 33106; End: 35664 Strand: -

Full Sequence      

MKIKSDYTNEPQWTELNVKSTLPKELVCLNEIAHNMWWAWTYQARNLFKSLDEDLYEQVG
HNPVLLLERLSLERLEAIVKDKTLMKHVDEVYKMFRAYMDVKPNAKRASVAYFSMEYGLN
QVLKIYSGGLGMLAGDYLKEASDSNVDLCAVGFLYRYGYFCQSLSMDGQQIAKYDAQQFN
SLPIEREYDKDGNQLVVEVPYRDYIVKALVWRVNVGRIKLYLLDTDNDFNSEYDRPITYA
LYGGDWENRLKQEILLGIGGMLTLKKLGIKKDVYHCNEGHAALCNLQRLCDYREEGLSFN
EAMELVRASGLYTVHTPVPAGHDYFDEELFGKYMGSYANKLGISWDEFIGMGRTNPDDHS
ERFCMSTFACNTCQEINGVSKLHGWVSQKMFAPLWKGYFAEENSVGYVTNGVHLPTWTAT
EWRKLYDKYYDKSFMSDQSNEDIWHAIYNVPDAEIWETRMALKVKLIKYIKDKFTQQWLR
NQGDPAKVVQVLEKINPNALMIGFCRRFATYKRAHLLFTDLERLDKIVNNPERPVLFFFS
GKAHPADGAGQGLIKKIFEISRMPQFLGKIIFLEDYDMQLARRLVSGVDIWMNTPTRPLE
ASGTSGEKAELNGVVNLSVLDGWYVEGYRKGAGWALPEKRTYKDQNYQDQLDAATIYSLL
ENEIAPLFFNKDAKTGYSKEWIQVVKNSIATIAPHYTMKRQLDDYFDKFYNRQAKRFAEL
CSKDNKLAKELAAWKEQVAEKWDAINVVAKNVDALHDVTTGKKAKLSFTIDEQGLKDAVG
LELVILYNTPVDDVNVFEVVPFKMVKSEGNCYTFEVEYNPNVAGSYKYGVRMYPKNSKLP
HRQDFAYVKWIG

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	124	707	4.3e-127	0.9020771513353115

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0058	GlgP	0.0	29	720	6	711	Glucan phosphorylase [Carbohydrate transport and metabolism].
TIGR02094	more_P_ylases	0.0	110	712	1	601	alpha-glucan phosphorylases. This family consists of known phosphorylases, and homologs believed to share the function of using inorganic phosphate to cleave an alpha 1,4 linkage between the terminal glucose residue and the rest of the polymer (maltodextrin, glycogen, etc.). The name of the glucose storage polymer substrate, and therefore the name of this enzyme, depends on the chain lengths and branching patterns. A number of the members of this family have been shown to operate on small maltodextrins, as may be obtained by utilization of exogenous sources. This family represents a distinct clade from the related family modeled by TIGR02093/pfam00343.
cd04299	GT35_Glycogen_Phosphorylase-like	0.0	29	799	1	773	proteins similar to glycogen phosphorylase. This family is most closely related to the oligosaccharide phosphorylase domain family and other unidentified sequences. Oligosaccharide phosphorylase catalyzes the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism.
pfam11897	DUF3417	1.61e-33	22	123	1	109	Protein of unknown function (DUF3417). This family of proteins are functionally uncharacterized. This protein is found in bacteria and archaea. Proteins in this family are typically between 145 to 860 amino acids in length. This protein is found associated with pfam00343. This protein has a conserved AYF sequence motif.
cd04300	GT35_Glycogen_Phosphorylase	6.71e-22	41	626	10	665	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
BBA29407.1	0.0	1	852	1	852
QUB40752.1	0.0	1	852	1	852
QUB83880.1	0.0	1	852	1	852
QUB70534.1	0.0	1	852	1	852
QUB87138.1	0.0	1	852	1	852

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C4M_A	5.61e-19	108	626	88	653	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]
7TM7_A	7.46e-19	127	626	121	672	ChainA, Alpha-1,4 glucan phosphorylase [Klebsiella pneumoniae subsp. pneumoniae HS11286],7TM7_B Chain B, Alpha-1,4 glucan phosphorylase [Klebsiella pneumoniae subsp. pneumoniae HS11286]
1L5V_A	2.23e-18	93	626	44	663	CrystalStructure of the Maltodextrin Phosphorylase complexed with Glucose-1-phosphate [Escherichia coli],1L5V_B Crystal Structure of the Maltodextrin Phosphorylase complexed with Glucose-1-phosphate [Escherichia coli],1L5W_A Crystal Structure of the Maltodextrin Phosphorylase Complexed with the Products of the Enzymatic Reaction between Glucose-1-phosphate and Maltotetraose [Escherichia coli],1L5W_B Crystal Structure of the Maltodextrin Phosphorylase Complexed with the Products of the Enzymatic Reaction between Glucose-1-phosphate and Maltotetraose [Escherichia coli],1L6I_A Crystal Structure of the Maltodextrin Phosphorylase complexed with the products of the enzymatic reaction between glucose-1-phosphate and maltopentaose [Escherichia coli],1L6I_B Crystal Structure of the Maltodextrin Phosphorylase complexed with the products of the enzymatic reaction between glucose-1-phosphate and maltopentaose [Escherichia coli],2ASV_A Chain A, Maltodextrin phosphorylase [Escherichia coli],2ASV_B Chain B, Maltodextrin phosphorylase [Escherichia coli],2AV6_A Chain A, Maltodextrin phosphorylase [Escherichia coli],2AV6_B Chain B, Maltodextrin phosphorylase [Escherichia coli],2AW3_A X-Ray studies on maltodextrin phosphorylase complexes: recognition of substrates and cathalitic mechanism of phosphorylase family [Escherichia coli],2AW3_B X-Ray studies on maltodextrin phosphorylase complexes: recognition of substrates and cathalitic mechanism of phosphorylase family [Escherichia coli],2AZD_A Chain A, Maltodextrin phosphorylase [Escherichia coli],2AZD_B Chain B, Maltodextrin phosphorylase [Escherichia coli]
1E4O_A	5.08e-18	93	626	44	663	Phosphorylaserecognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli],1E4O_B Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli],1QM5_A Phosphorylase recognition and phosphorylysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli],1QM5_B Phosphorylase recognition and phosphorylysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli]
2ECP_A	8.81e-18	93	626	44	663	TheCrystal Structure Of The E. Coli Maltodextrin Phosphorylase Complex [Escherichia coli],2ECP_B The Crystal Structure Of The E. Coli Maltodextrin Phosphorylase Complex [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9YGA7	3.60e-206	18	852	8	827	Maltodextrin phosphorylase OS=Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) OX=523849 GN=malP PE=1 SV=1
O66932	8.49e-178	31	712	12	686	Glycogen phosphorylase OS=Aquifex aeolicus (strain VF5) OX=224324 GN=glgP PE=3 SV=1
Q7U078	4.65e-171	18	848	9	860	Glycogen phosphorylase OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=glgP PE=3 SV=1
P9WMW1	6.55e-171	18	848	9	860	Glycogen phosphorylase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=glgP PE=1 SV=1
P9WMW0	2.58e-170	18	848	9	860	Glycogen phosphorylase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=glgP PE=3 SV=1

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
1.000058	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003731_00285.