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Database: UniProt
Entry: Q7MMP7_VIBVY
LinkDB: Q7MMP7_VIBVY
Original site: Q7MMP7_VIBVY 
ID   Q7MMP7_VIBVY            Unreviewed;       552 AA.
AC   Q7MMP7;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   24-JAN-2024, entry version 127.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:BAC93784.1};
GN   OrderedLocusNames=VV1020 {ECO:0000313|EMBL:BAC93784.1};
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC93784.1, ECO:0000313|Proteomes:UP000002675};
RN   [1] {ECO:0000313|EMBL:BAC93784.1, ECO:0000313|Proteomes:UP000002675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016 {ECO:0000313|EMBL:BAC93784.1,
RC   ECO:0000313|Proteomes:UP000002675};
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L., Liu Y.M.,
RA   Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T., Hor L.I.,
RA   Tsai S.F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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}.
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DR   EMBL; BA000037; BAC93784.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7MMP7; -.
DR   STRING; 672.VV93_v1c09430; -.
DR   KEGG; vvy:VV1020; -.
DR   eggNOG; COG0033; Bacteria.
DR   HOGENOM; CLU_016950_8_1_6; -.
DR   OMA; AFNEDHI; -.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05801; PGM_like3; 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; IPR045244; PGM.
DR   InterPro; IPR005852; PGM_a-D-Glc-sp.
DR   NCBIfam; TIGR01132; pgm; 1.
DR   PANTHER; PTHR22573:SF57; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 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   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}.
FT   DOMAIN          43..181
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          213..318
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          324..442
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          494..541
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   552 AA;  59537 MW;  6033C2F242AE9AE0 CRC64;
     MSLMAMHPRA GQKALQEDLH NIPALVANYF LLQPDPTNPA HKVEFGTSGH RGCADKSTFN
     EHHILAIAQA VAEVRAEQGT TGPLFVGKDT HALSEPAFST VVEVLIANGV TVIVQEQNGY
     TPTPGISHAI LTYNLQHEEK ADGIVITPSH NPPQDGGIKY NPTHGGPAEG ELTQRIEDRA
     NVLIAEGLQG VKRMPLAQAK ASSLFVEQDL VKPYVDDLVN VIDMAAIQKA GLKLGVDPLG
     GSGIDYWRQI GTAYNLDLTL VSEAIDPSFQ FMSLDKDGVV RMDCSSPYAM AGLLALKDQY
     DLAFGNDPDY DRHGIVTPTK GLMNPNHFLA VCIDYLYRHR QGWAADVAVG KTLVSSAMID
     RVVADLGREL CEVPVGFKWF VDGLYNGKFG FGGEESAGAS FLRQDGTPWS TDKDGIILCL
     LAAEITAVTG KNPQQYYDEL AAKHGESQYS RIQAVANGPQ KEVLKKLSAE MVKAETLAGD
     EITARLTHAP GNGAAIGGLK VTTANGWFAA RPSGTEDIYK IYCESFKGAE HLKQIELEAQ
     EIVNQVFAEA GL
//
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