ID U3A4F7_VIBPR Unreviewed; 567 AA.
AC U3A4F7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:GAD68222.1};
GN Name=pgm {ECO:0000313|EMBL:GAD68222.1};
GN ORFNames=VPR01S_12_00300 {ECO:0000313|EMBL:GAD68222.1};
OS Vibrio proteolyticus NBRC 13287.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219065 {ECO:0000313|EMBL:GAD68222.1, ECO:0000313|Proteomes:UP000016570};
RN [1] {ECO:0000313|EMBL:GAD68222.1, ECO:0000313|Proteomes:UP000016570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13287 {ECO:0000313|EMBL:GAD68222.1,
RC ECO:0000313|Proteomes:UP000016570};
RA Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Vibrio proteolyticus NBRC 13287.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:GAD68222.1}.
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DR EMBL; BATJ01000012; GAD68222.1; -; Genomic_DNA.
DR RefSeq; WP_021706193.1; NZ_BATJ01000012.1.
DR AlphaFoldDB; U3A4F7; -.
DR STRING; 1219065.VPR01S_12_00300; -.
DR eggNOG; COG1109; Bacteria.
DR Proteomes; UP000016570; 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; IPR005843; A-D-PHexomutase_C.
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 Pfam; PF00408; PGM_PMM_IV; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000016570}.
FT DOMAIN 40..179
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 204..309
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 321..439
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 512..535
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 567 AA; 61989 MW; 55F74858BF8C52AB CRC64;
MEKITQWLER DPDPRTQQEL KALIEANNTA ELDDRFKSRL EFGTAGLRGK VGCGPNRMNR
LVIQETATGL GHYLTEQIPQ AAHRGVVIGY DGRPDSQQFA HDTAAALAAQ GIKVYLTHKV
APTPVVAFGV MHFGAAAAVV VTASHNPPEY NGFKVYWENG AQIIPPHDSG IAAKIDQAAT
QPLALMPLDQ AEAQGLLVWL TDDYYQTYRQ VMNNNELLAN HTKPDAIGLA YTAMHGVGAD
MAETLLKDAG FHQVYSVVEQ REPDGAFPTV NFPNPEEAGA MDMVMALAAK HGAQLACAND
PDADRFAVAV RKPDGDYQML TGDQVGTLFG HYLLAKSPTP DKQLVGNTIV SSSLLSKVAQ
AAGAEYYQTL TGFKWLTNVA MQKQSDQHQF LFAYEEALGY TVGNKVWDKD GLSALVAFAQ
LAAELYSQGK TIWDQLETIY RQHGMYINAQ RSIALDPGAP PVGDKLRANP PSEIAGMNVE
VIEDFKTSTR TTIDGKTLPI DLPVSDVLIY HLAGGARVVV RPSGTEPKLK CYYEVVGQFT
DSDSYERAYQ RAEAQMNELI DFHQTSL
//
