dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

UBA10281 sp900767495

Lineage

Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; UBA10281; UBA10281 sp900767495

CAZyme ID

MGYG000000473_00715

CAZy Family

GH95

CAZyme Description

Phosphoglycolate phosphatase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
972	MGYG000000473_23\|CGC2	108927.85	5.5012

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000473	1843328	MAG	Fiji	Oceania

Gene Location

Start: 17552; End: 20470 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000000473_00715.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH95	222	948	7.7e-179	0.9736842105263158

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR01990	bPGM	2.77e-74	4	188	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	2.50e-60	2	186	1	184	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).
cd02598	HAD_BPGM	3.64e-49	4	206	1	166	beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM). Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.
COG0637	YcjU	3.97e-45	1	213	1	219	Beta-phosphoglucomutase or related phosphatase, HAD superfamily [Carbohydrate transport and metabolism, General function prediction only].
pfam14498	Glyco_hyd_65N_2	1.08e-30	222	453	3	233	Glycosyl hydrolase family 65, N-terminal domain. This domain represents a domain found to the N-terminus of the glycosyl hydrolase 65 family catalytic domain.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AHW58797.1	2.72e-119	222	945	30	751
QIA08082.1	3.94e-118	222	959	30	761
QDH81513.1	3.89e-115	212	951	22	763
BBE15989.1	1.21e-114	222	945	30	752
ADX05719.1	1.39e-114	235	960	50	760

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4UFC_A	4.85e-100	235	945	36	741	Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus]
7KMQ_A	1.42e-97	235	950	55	762	ChainA, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306],7KMQ_B Chain B, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306]
2RDY_A	8.41e-82	222	960	7	765	ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125]
2EAB_A	1.12e-55	236	949	52	855	Crystalstructure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAB_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAC_A Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum],2EAC_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum]
2EAD_A	6.53e-55	236	949	52	855	ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8L7W8	2.99e-89	235	938	66	805	Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1
A2R797	3.75e-65	223	933	26	765	Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1
Q5AU81	1.92e-51	239	921	47	772	Alpha-fucosidase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=afcA PE=1 SV=1
O06995	4.68e-41	3	217	2	217	Beta-phosphoglucomutase OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdM PE=1 SV=1
Q2USL3	3.77e-40	235	945	32	714	Probable alpha-fucosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=afcA PE=3 SV=2

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
1.000027	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000473_00715.

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