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Database: UniProt
Entry: C9P863_VIBME
LinkDB: C9P863_VIBME
Original site: C9P863_VIBME 
ID   C9P863_VIBME            Unreviewed;       568 AA.
AC   C9P863;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=Phosphosugar mutase {ECO:0000313|EMBL:EEX36390.1};
GN   ORFNames=VIB_002705 {ECO:0000313|EMBL:EEX36390.1};
OS   Vibrio metschnikovii CIP 69.14.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=675813 {ECO:0000313|EMBL:EEX36390.1, ECO:0000313|Proteomes:UP000005604};
RN   [1] {ECO:0000313|EMBL:EEX36390.1, ECO:0000313|Proteomes:UP000005604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 69.14 {ECO:0000313|EMBL:EEX36390.1,
RC   ECO:0000313|Proteomes:UP000005604};
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA   Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D.,
RA   Vonstein V.;
RL   Submitted (OCT-2009) 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}.
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DR   EMBL; ACZO01000007; EEX36390.1; -; Genomic_DNA.
DR   RefSeq; WP_004396993.1; NZ_ACZO01000007.1.
DR   AlphaFoldDB; C9P863; -.
DR   STRING; 675813.VIB_002705; -.
DR   GeneID; 79889694; -.
DR   eggNOG; COG1109; Bacteria.
DR   Proteomes; UP000005604; 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:UP000005604}.
FT   DOMAIN          41..177
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          204..310
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          322..441
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          505..548
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   568 AA;  61983 MW;  56A06F806D0CDB70 CRC64;
     MNNNVTLWLA RDPDLRTRKE LQTLIDNQQQ DEIEDRFKSR LEFGTAGLRG KVGCGPNRMN
     RLVIQETAVG LGHYLIQQVD NAKQRGVVIG YDGRPDSQQF AQDTASVLTA LGIKVYLTYK
     VAPTPVVAFG VKHLQAAAAV VVTASHNPPE YNGFKVYWEN GAQIIAPHDS GIANQIDLAA
     TQSIPTLGLD KAQQQGLLVW LQDDYYQTYR QTINASPLLQ HHTDPSSVTI AYTAMHGVGA
     EMAETLLADA GFNKVMSVKE QREPDGSFPT VNFPNPEEAG AMDRVIALAE SVNAELACAN
     DPDADRFAVA VAKPTGGYQM LTGDQVGALL GDYLLRHTAH QAPLVGNTIV SSSLLSKIAA
     AHGAVYYQTL TGFKWLTNVA MAKQSEQHPF LFAYEEALGY TVGNSVWDKD GLSAMVAFAQ
     LAAELYSQGK TIWDQLEALY RQHGLYVTAQ RSIALAPDTP PIGDRLRATP PHTIAGKPVV
     SYDDLKLAVR HHQDGTTEPL TWPSSDVLIY HLQDGARVIV RPSGTEPKLK CYYEVVGTFA
     ADESFAEAEL RAEEQMALLI SEHQSSLV
//
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