ID Q87IS1_VIBPA Unreviewed; 564 AA.
AC Q87IS1;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Putative phosphomannomutase {ECO:0000313|EMBL:BAC61878.1};
GN OrderedLocusNames=VPA0535 {ECO:0000313|EMBL:BAC61878.1};
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC61878.1, ECO:0000313|Proteomes:UP000002493};
RN [1] {ECO:0000313|EMBL:BAC61878.1, ECO:0000313|Proteomes:UP000002493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(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; BA000032; BAC61878.1; -; Genomic_DNA.
DR RefSeq; NP_800045.1; NC_004605.1.
DR RefSeq; WP_005482641.1; NC_004605.1.
DR AlphaFoldDB; Q87IS1; -.
DR GeneID; 1191223; -.
DR KEGG; vpa:VPA0535; -.
DR PATRIC; fig|223926.6.peg.3476; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_0_6; -.
DR Proteomes; UP000002493; Chromosome 2.
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:UP000002493}.
FT DOMAIN 41..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 208..309
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 321..438
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 509..532
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 564 AA; 61660 MW; 440F1F166F251DC9 CRC64;
MTALITQWLA RDPDPKTREE LQHLVDTNNE QELSDRFGSR LAFGTAGLRG KVGAGPNRMN
RLVIQETATG LGHYLLEQVQ DAASRGVVIG YDGRPDSKQF AHDTASVLTA LGIKVYLTYQ
VAATPIVAFG VRTMNAAAAV VVTASHNPPE YNGFKVYWEN GAQIIPPHDS GIAAKIDEAT
TKPLPLMSLD DAKQQGLLVW LEDDYYQTYR KTMNENALLT PDSNTDISIA YTAMHGVGAD
MAETLLADAG FKKVASVAEQ REPDGTFPTV NFPNPEEAGA MDMVMALGKS VDADIACAND
PDADRFAVAV KRPDGEYQML TGDQVGSLFG DYLLEQQPNS LVGNTIVSSR LLSSIAKAHG
AEYYQTLTGF KWLTNVAMSQ ETEQHPFLFA YEEALGYTVG NKVWDKDGLS AIVAFSQLTG
KLKAQGKTLW DKLEALYRQH GFYFNAQRSI ALDPNSPPIG DKLRANPPSE IAGKKVSVTE
DLKTSVRTFE DGSEETIDLP ASDVLIYHLE DKSRVIVRPS GTEPKLKCYY EVISDFPADM
SYEQAQQAAE AKMNALIDAH QKSL
//
