GMHA_VIBCH
ID GMHA_VIBCH Reviewed; 191 AA.
AC Q9KPY2;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Phosphoheptose isomerase;
DE EC=5.3.1.28;
DE AltName: Full=Sedoheptulose 7-phosphate isomerase;
GN Name=gmhA; OrderedLocusNames=VC_2230;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
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.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann 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).
RN [2]
RP BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.
RX PubMed=12101286; DOI=10.1099/00221287-148-7-1979;
RA Valvano M.A., Messner P., Kosma P.;
RT "Novel pathways for biosynthesis of nucleotide-activated glycero-manno-
RT heptose precursors of bacterial glycoproteins and cell surface
RT polysaccharides.";
RL Microbiology 148:1979-1989(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=16477602; DOI=10.1002/prot.20908;
RA Seetharaman J., Rajashankar K.R., Solorzano V., Kniewel R., Lima C.D.,
RA Bonanno J.B., Burley S.K., Swaminathan S.;
RT "Crystal structures of two putative phosphoheptose isomerases.";
RL Proteins 63:1092-1096(2006).
CC -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in
CC D-glycero-D-manno-heptose 7-phosphate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-
CC heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate;
CC Xref=Rhea:RHEA:27489, ChEBI:CHEBI:57483, ChEBI:CHEBI:60203,
CC ChEBI:CHEBI:60204; EC=5.3.1.28;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-
CC phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and
CC D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-
CC phosphate: step 1/1.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The reaction produces a racemic mixture of D-glycero-
CC alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-
CC phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily. {ECO:0000305}.
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DR EMBL; AE003852; AAF95374.1; -; Genomic_DNA.
DR PIR; B82104; B82104.
DR RefSeq; NP_231861.1; NC_002505.1.
DR RefSeq; WP_000284054.1; NZ_LT906614.1.
DR PDB; 1X94; X-ray; 2.50 A; A/B=1-191.
DR PDBsum; 1X94; -.
DR AlphaFoldDB; Q9KPY2; -.
DR SMR; Q9KPY2; -.
DR STRING; 243277.VC_2230; -.
DR DNASU; 2613270; -.
DR EnsemblBacteria; AAF95374; AAF95374; VC_2230.
DR GeneID; 57740854; -.
DR KEGG; vch:VC_2230; -.
DR PATRIC; fig|243277.26.peg.2127; -.
DR eggNOG; COG0279; Bacteria.
DR HOGENOM; CLU_080999_4_0_6; -.
DR OMA; FLAHKEA; -.
DR BioCyc; VCHO:VC2230-MON; -.
DR BRENDA; 5.3.1.28; 6626.
DR UniPathway; UPA00041; UER00436.
DR UniPathway; UPA00958; -.
DR EvolutionaryTrace; Q9KPY2; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0008968; F:D-sedoheptulose 7-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:2001061; P:D-glycero-D-manno-heptose 7-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05006; SIS_GmhA; 1.
DR HAMAP; MF_00067; GmhA; 1.
DR InterPro; IPR035461; GmhA/DiaA.
DR InterPro; IPR004515; Phosphoheptose_Isoase.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF13580; SIS_2; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR TIGRFAMs; TIGR00441; gmhA; 1.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase;
KW Lipopolysaccharide biosynthesis; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..191
FT /note="Phosphoheptose isomerase"
FT /id="PRO_0000136548"
FT DOMAIN 37..191
FT /note="SIS"
FT BINDING 52..54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 93..94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119..121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT HELIX 3..21
FT /evidence="ECO:0007829|PDB:1X94"
FT HELIX 24..41
FT /evidence="ECO:0007829|PDB:1X94"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1X94"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1X94"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1X94"
FT HELIX 55..70
FT /evidence="ECO:0007829|PDB:1X94"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1X94"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:1X94"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:1X94"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:1X94"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:1X94"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1X94"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1X94"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:1X94"
FT HELIX 168..189
FT /evidence="ECO:0007829|PDB:1X94"
SQ SEQUENCE 191 AA; 20646 MW; B5A57D89F437FED0 CRC64;
MYQDLIRSEL TEAADVLQKF LSDDHNIAQI EAAAKLIADS FKQGGKVLSC GNGGSHCDAM
HFAEELTGRY RENRPGYPGI AISDPSHLSC VSNDFGYDYV FSRYVEAVGA KGDVLFGLST
SGNSGNILKA IEAAKAKGMK TIALTGKDGG KMAGLADVEI RVPHFGYADR IQEVHIKIIH
IIIQLIEKEM A
