dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Lacrimispora sp902363835

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lacrimispora; Lacrimispora sp902363835

CAZyme ID

MGYG000000152_03427

CAZy Family

GH65

CAZyme Description

Pyrophosphatase PpaX

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
990	MGYG000000152_16\|CGC1	112792.48	5.4662

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000152	6260407	Isolate	United Kingdom	Europe

Gene Location

Start: 16170; End: 19142 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000000152_03427.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH65	319	711	4.7e-135	0.9946236559139785

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1554	ATH1	0.0	13	780	7	772	Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
pfam03632	Glyco_hydro_65m	1.45e-141	319	714	1	387	Glycosyl hydrolase family 65 central catalytic domain. This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom. The catalytic domain also forms the majority of the dimerization interface.
PRK13807	PRK13807	1.01e-129	17	774	10	754	maltose phosphorylase; Provisional
TIGR01990	bPGM	3.08e-75	783	967	1	185	beta-phosphoglucomutase. This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
TIGR02009	PGMB-YQAB-SF	6.58e-61	781	966	1	185	beta-phosphoglucomutase family hydrolase. This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
SET49151.1	1	990	1	990
ADL03489.1	1	989	1	989
QRV18359.1	1	989	1	989
QMW77936.1	5	761	4	760
QIB53418.1	5	761	4	760

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WIQ_A	2.93e-134	15	749	6	736	Crystalstructure of kojibiose phosphorylase complexed with kojibiose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_A Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_B Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_C Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_D Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903]
4KTR_A	3.66e-101	17	769	14	753	ChainA, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_B Chain B, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_C Chain C, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_D Chain D, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_E Chain E, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_F Chain F, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_G Chain G, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_H Chain H, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10]
4KTP_A	7.06e-101	17	769	14	753	ChainA, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTP_B Chain B, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10]
1H54_A	4.13e-77	13	766	6	748	ChainA, Maltose Phosphorylase [Levilactobacillus brevis],1H54_B Chain B, Maltose Phosphorylase [Levilactobacillus brevis]
7FE3_A	1.76e-56	40	727	43	662	ChainA, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE3_B Chain B, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE3_C Chain C, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE4_A Chain A, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE4_B Chain B, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE4_C Chain C, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P77154	2.95e-166	19	764	7	725	Kojibiose phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=ycjT PE=1 SV=1
Q8RBL8	5.04e-134	12	749	12	751	Kojibiose phosphorylase OS=Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) OX=273068 GN=kojP PE=3 SV=1
Q8L163	4.85e-124	17	769	19	775	Kojibiose phosphorylase OS=Thermoanaerobacter brockii OX=29323 GN=kojP PE=1 SV=1
Q8L164	2.60e-113	15	769	13	769	Alpha,alpha-trehalose phosphorylase OS=Thermoanaerobacter brockii OX=29323 GN=treP PE=1 SV=1
D6XZ22	6.18e-101	17	769	14	753	1,2-alpha-glucosylglycerol phosphorylase OS=Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10) OX=439292 GN=Bsel_2816 PE=1 SV=1

SignalP and Lipop Annotations help

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 help

There is no transmembrane helices in MGYG000000152_03427.

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