ID Q9KUB2_VIBCH Unreviewed; 470 AA.
AC Q9KUB2;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase, putative {ECO:0000313|EMBL:AAF93777.1};
GN OrderedLocusNames=VC_0611 {ECO:0000313|EMBL:AAF93777.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF93777.1, ECO:0000313|Proteomes:UP000000584};
RN [1] {ECO:0000313|EMBL:AAF93777.1, ECO:0000313|Proteomes:UP000000584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961
RC {ECO:0000313|Proteomes:UP000000584};
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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}.
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DR EMBL; AE003852; AAF93777.1; -; Genomic_DNA.
DR PIR; F82302; F82302.
DR RefSeq; NP_230260.1; NC_002505.1.
DR RefSeq; WP_000589191.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KUB2; -.
DR STRING; 243277.VC_0611; -.
DR DNASU; 2615399; -.
DR EnsemblBacteria; AAF93777; AAF93777; VC_0611.
DR KEGG; vch:VC_0611; -.
DR PATRIC; fig|243277.26.peg.582; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_6; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004614; F:phosphoglucomutase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR CDD; cd05800; PGM_like2; 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; 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; 2.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000584}.
FT DOMAIN 2..136
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 162..262
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 267..378
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 414..466
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 470 AA; 52284 MW; 06F888DF5059C075 CRC64;
MIKFGTGGWR AFIGEEFTKD NVRLVAQALA NIIHHEQAAN EGFVIGYDRR FLSDKAGRWF
AEVLAANGVV VSFIDKFVPT PVVMFKAKAM DCAYSACITA SHNPADYNGI KVFIRGGRDA
DEVITQKIEQ QIATLTLQDV KSIDFDQAVN DKLIDIINPM NEFVDSIINF IDIEAIKKAN
LRVLIDPMFG VAKNALQTVL INGRCDVDVI NDGKNPDFGG LMPSPSAATL YRLKHLVKHE
GYDIGIGTDG DADRLGIIDE KGNFIHPNEV LILLYYYLLE YKGWKGSVVR NIATTHLLDK
IAADHGERCF EVPVGFKHIS SQMEADDSLI GGESSGGLTI RGHIKGKDGV FASSLLVEMI
SVTGKKLSEL LTEIYDRYGY AYTAEGDCKF KPAQRDEIYN KVYIEKKLPE FEFDIDKVSY
EDGAKVYFKN GGWVIARFSG TEPLLRIFAE MADKDTAERV LQQMKAFLAL
//
