ID R6MVJ9_9CLOT Unreviewed; 573 AA.
AC R6MVJ9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Phosphoglucomutase {ECO:0000256|ARBA:ARBA00039995};
DE AltName: Full=Alpha-phosphoglucomutase {ECO:0000256|ARBA:ARBA00041467};
DE AltName: Full=Glucose phosphomutase {ECO:0000256|ARBA:ARBA00041398};
GN ORFNames=BN565_02030 {ECO:0000313|EMBL:CDB89862.1};
OS Clostridium sp. CAG:253.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262785 {ECO:0000313|EMBL:CDB89862.1, ECO:0000313|Proteomes:UP000018071};
RN [1] {ECO:0000313|EMBL:CDB89862.1, ECO:0000313|Proteomes:UP000018071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:253 {ECO:0000313|Proteomes:UP000018071};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005164}.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDB89862.1}.
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DR EMBL; CBEI010000103; CDB89862.1; -; Genomic_DNA.
DR AlphaFoldDB; R6MVJ9; -.
DR STRING; 1262785.BN565_02030; -.
DR Proteomes; UP000018071; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05799; PGM2; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326}.
FT DOMAIN 43..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 207..312
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 326..450
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 573 AA; 63895 MW; 7AA810769C0DE4F4 CRC64;
MDYKEIYESW LSNPYFDEET KAELKAIADD DNEIKERFYQ DLEFGTAGLR GVIGAGTNRM
NIYTVRKATQ GLANYIIKAG KQSQGVAIAY DSRHMSPEFA DEAALCLAAN GIKAYVFESL
RPTPELSYAV RELKCVAGIN VTASHNPPEY NGYKVYWEDG AQITPPHDTG IMDEVKAVTD
YNTVKTMAKE DAVKQGLYQQ IGKDIDDKYI EELKKQVIHW DSIKEMGDKL KIVYTPLHGT
GNIPARRVLE ELGFKNVYVV PEQELPDGDF PTVSYPNPEA AEAFELALKL AKEKDADLVL
ATDPDADRLG VYVKDTKSGE YITLTGNMSG CLLADYEISQ IKETKGLPDD GKLIKTIVTS
NLADEIAKYY GVELIEVLTG FKYIGQQILN FETTGKGTYL FGFEESYGCL IGTHARDKDA
IVATMALCEA AAYYKTKNMT LWDAMIAMYE RYGYCKDGVK AVTMKGIEGL AKIQEIMSDL
RKNPPKEIDG HKVLSFRDYQ ADTITDLATG EVKPTGLPKS NVLYFDMEDN VWMCVRPSGT
EPKIKFYYGV VGTSLEDADK KSEQMAKAVD DLI
//
