CAZyme Information: MGYG000004762_00117

Basic Information

• Species: Catenibacillus sp900553975
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Catenibacillus; Catenibacillus sp900553975
• CAZyme ID: MGYG000004762_00117
• CAZy Family: GH36
• CAZyme Description: Phosphoglycolate phosphatase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
804	MGYG000004762_1|CGC3	91329.14	5.1313

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004762	3086790	MAG	China	Asia

• Gene Location: Start: 139175; End: 141589 Strand: -

Full Sequence      

MIRLNFETKGSGNDCCQACGLLVCGQEYTIDYYKSSWGREFEPQQFKWKAGETFNMTCTT
GRSSHGVHPFFRISSDSGHILSVLVAWSGTWYVEIDGHGTIEVGLPDIRVLPKKYDDTHT
QDEIQTKDGQAGCFKFPAVYIFQAWDGDWDCLTQKLHDYGRSYLYPEAGELPVEWNHWWT
FEDALINENVFLENAAAAKAMGVELCTLDAGWYGRPGNIHWSRQQGDWAMVNEQRFPHGL
AYISKKLHEMNMKFGLWMEPEAIGQDSRLIGSHPEFEAVSEGKHYENPYICLGNDSAAQW
LFQMLCKMIETSGCDWMKLDFNMDPGAGCSRMDHNHHEKDGLFWHYQGYYDILNKIKNKY
PQLTLENCASGGLRCDIGLLSCVNQTFLSDVDETGHSLNSFYELSRFIPPEHILHWAWSQ
TRTYDDGSQAFPGFEIREDTPQDLIRYTIRAAMPHALGFSRDFASMSERNRDIFRQEIHY
YKTVVRPVIRRARLFHLQNARGCMVLQYAGMDGHAEGRQLLFVFCMRDFCEKQVIVKPKA
LDPARTYRIVDRDGIFNGQSSGKALMETGFLVSSGPQRAWIFELIEEDETMSKKYKGVIF
DLDGVICFTDHYHYLAWKTVADKLGIYFDEVINNRLRGVSRMESLEIILEKYDKPLTQDE
KVALAEEKNGVYKELLKNMSPADLSSEVKETLDGLRAKGLKLAIGSSSKNTQFILERIGL
KGYFDAVSDGNNITNSKPDPEVFIKAAQFIGENPEDCLVVEDAYAGVDGACAGGFDSAAI
GDASSYEKATYSMKTFGDLMGICE

Enzyme Prediction     

No EC number prediction in MGYG000004762_00117.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH36	25	570	3.7e-93	0.7558139534883721

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR01990	bPGM	1.86e-82	597	781	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	7.14e-65	595	780	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).
cd14791	GH36	6.51e-64	170	483	1	299	glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
cd02598	HAD_BPGM	4.08e-55	597	799	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	8.81e-42	594	789	1	194	Beta-phosphoglucomutase or related phosphatase, HAD superfamily [Carbohydrate transport and metabolism, General function prediction only].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAJ64607.1	7.86e-114	29	572	143	676
ABQ89756.1	1.04e-111	28	577	134	674
QHW33776.1	4.63e-111	32	575	58	585
ALS29850.1	2.75e-110	4	591	69	644
ABU59612.1	8.59e-110	28	585	134	682

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1O03_A	5.39e-40	595	767	2	175	Structureof Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 6-phosphate [Lactococcus lactis],1O08_A Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 1-phosphate [Lactococcus lactis],1Z4N_A Structure of beta-phosphoglucomutase with inhibitor bound alpha-galactose 1-phosphate cocrystallized with Fluoride [Lactococcus lactis],1Z4N_B Structure of beta-phosphoglucomutase with inhibitor bound alpha-galactose 1-phosphate cocrystallized with Fluoride [Lactococcus lactis],1Z4O_A Structure of beta-phosphoglucomutase with inhibitor bound alpha-galactose 1-phosphate [Lactococcus lactis],1Z4O_B Structure of beta-phosphoglucomutase with inhibitor bound alpha-galactose 1-phosphate [Lactococcus lactis],1ZOL_A native beta-PGM [Lactococcus lactis],2WF5_A Structure of Beta-Phosphoglucomutase inhibited with Glucose-6-phosphate and trifluoromagnesate [Lactococcus lactis],2WF6_A Structure of Beta-Phosphoglucomutase inhibited with Glucose-6-phosphate and Aluminium tetrafluoride [Lactococcus lactis],2WF7_A Structure of Beta-Phosphoglucomutase inhibited with Glucose-6- phosphonate and Aluminium tetrafluoride [Lactococcus lactis],2WF8_A Structure of Beta-Phosphoglucomutase inhibited with Glucose-6- phosphate, Glucose-1-phosphate and Beryllium trifluoride [Lactococcus lactis],2WF9_A Structure of Beta-Phosphoglucomutase inhibited with Glucose-6- phosphate, and Beryllium trifluoride, crystal form 2 [Lactococcus lactis],2WFA_A Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation. [Lactococcus lactis],2WHE_A Structure of native Beta-Phosphoglucomutase in an open conformation without bound ligands. [Lactococcus lactis],3ZI4_A The structure of Beta-phosphoglucomutase Inhibited With Glucose-6-phosphate and Scandium Tetrafluoride [Lactococcus lactis],4C4R_A Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride [Lactococcus lactis],4C4S_A Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride [Lactococcus lactis],4C4T_A Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and aluminium tetrafluoride [Lactococcus lactis],6H8U_A Beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 1.9 A. [Lactococcus lactis subsp. lactis Il1403],6H8V_A Beta-phosphoglucomutase from Lactococcus lactis in an open conformer in the P21 spacegroup to 1.8 A. [Lactococcus lactis subsp. lactis Il1403],6H8V_B Beta-phosphoglucomutase from Lactococcus lactis in an open conformer in the P21 spacegroup to 1.8 A. [Lactococcus lactis subsp. lactis Il1403],6H8W_A Beta-phosphoglucomutase from Lactococcus lactis in an open conformer complexed with aluminium tetrafluoride to 1.9 A. [Lactococcus lactis subsp. lactis Il1403],6H8X_A Beta-phosphoglucomutase from Lactococcus lactis in an open conformer complexed with magnesium trifluoride to 1.8 A. [Lactococcus lactis subsp. lactis Il1403],6H8X_B Beta-phosphoglucomutase from Lactococcus lactis in an open conformer complexed with magnesium trifluoride to 1.8 A. [Lactococcus lactis subsp. lactis Il1403],6H93_A Beta-phosphoglucomutase from Lactococcus lactis with inorganic phosphate bound in an open conformer to 1.8 A. [Lactococcus lactis subsp. lactis Il1403],6H93_B Beta-phosphoglucomutase from Lactococcus lactis with inorganic phosphate bound in an open conformer to 1.8 A. [Lactococcus lactis subsp. lactis Il1403],6QZG_A Beta-glucose 1,6-bisphosphonate bound to wild type beta-phosphoglucomutse in an open conformation. [Lactococcus lactis subsp. lactis Il1403],6QZG_B Beta-glucose 1,6-bisphosphonate bound to wild type beta-phosphoglucomutse in an open conformation. [Lactococcus lactis subsp. lactis Il1403],6YDL_A Substrate-free beta-phosphoglucomutase from Lactococcus lactis [Lactococcus lactis subsp. lactis Il1403],6YDM_A beta-phosphoglucomutase from Lactococcus lactis with citrate, tris and acetate bound [Lactococcus lactis subsp. lactis Il1403],6YDM_B beta-phosphoglucomutase from Lactococcus lactis with citrate, tris and acetate bound [Lactococcus lactis subsp. lactis Il1403]
6HDH_A	1.37e-39	595	767	2	175	R49Kvariant of beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 1.6 A. [Lactococcus lactis subsp. lactis Il1403],6HDH_B R49K variant of beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 1.6 A. [Lactococcus lactis subsp. lactis Il1403],6HDJ_A R49K variant of beta-phosphoglucomutase from Lactococcus lactis complexed aluminium tetrafluoride and beta-G6P to 1.2 A. [Lactococcus lactis subsp. lactis Il1403],6HDL_A R49K variant of beta-phosphoglucomutase from Lactococcus lactis complexed with magnesium trifluoride and beta-G6P to 1.2 A. [Lactococcus lactis subsp. lactis Il1403]
5OK0_A	2.35e-39	595	767	2	175	Structureof the D10N mutant of beta-phosphoglucomutase from Lactococcus lactis trapped with native reaction intermediate beta-glucose 1,6-bisphosphate to 2.2A resolution. [Lactococcus lactis],5OK1_A D10N variant of beta-phosphoglucomutase from Lactococcus lactis trapped with native beta-glucose 1,6-bisphosphate intermediate to 1.9A resolution. [Lactococcus lactis],5OK2_A Structure of the D10N mutant of beta-phosphoglucomutase from Lactococcus lactis inhibited with glucose 6-phosphate and tetrafluoroaluminate to 1.1A resolution. [Lactococcus lactis]
5OJZ_A	2.49e-39	595	767	2	175	D10Nvariant of beta-phosphoglucomutase from Lactococcus lactis inhibited by a beryllium triflouride phosphoenzyme analogue to 1.3A resolution. [Lactococcus lactis]
6H8Y_A	2.56e-39	595	767	2	175	T16Avariant of beta-phosphoglucomutase from Lactococcus lactis in an open conformer complexed with aluminium tetrafluoride to 1.9 A. [Lactococcus lactis subsp. lactis Il1403],6H8Z_A T16A variant of beta-phosphoglucomutase from Lactococcus lactis in an open conformer complexed with magnesium trifluoride to 1.6 A. [Lactococcus lactis subsp. lactis Il1403],6H94_A T16A variant of beta-phosphoglucomutase from Lactococcus lactis with phosphate and TRIS bound in an open conformer to 1.5 A. [Lactococcus lactis subsp. lactis Il1403]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P71447	7.52e-39	595	767	2	175	Beta-phosphoglucomutase OS=Lactococcus lactis subsp. lactis (strain IL1403) OX=272623 GN=pgmB PE=1 SV=2
O06995	1.32e-34	596	799	2	207	Beta-phosphoglucomutase OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdM PE=1 SV=1
G1UB44	2.67e-32	61	570	226	712	Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1
P77366	7.16e-32	594	781	2	191	Beta-phosphoglucomutase OS=Escherichia coli (strain K12) OX=83333 GN=ycjU PE=1 SV=1
P27756	1.29e-29	28	572	184	703	Alpha-galactosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=aga PE=3 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
1.000009	0.000031	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004762_00117.