GMHA_BURPS
ID GMHA_BURPS Reviewed; 197 AA.
AC Q93UJ2; Q63R78;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Phosphoheptose isomerase;
DE EC=5.3.1.28;
DE AltName: Full=Sedoheptulose 7-phosphate isomerase;
GN Name=gmhA; OrderedLocusNames=BPSL2795;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11119486; DOI=10.1128/iai.69.1.34-44.2001;
RA Reckseidler S.L., DeShazer D., Sokol P.A., Woods D.E.;
RT "Detection of bacterial virulence genes by subtractive hybridization:
RT identification of capsular polysaccharide of Burkholderia pseudomallei as a
RT major virulence determinant.";
RL Infect. Immun. 69:34-44(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
RN [3]
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ZINC AND
RP D-GLYCERO-ALPHA-D-MANNO-HEPTOSE 7-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, REACTION MECHANISM, AND MUTAGENESIS OF ASP-61; HIS-64;
RP GLU-68; ASP-98; THR-124 AND GLN-175.
RX PubMed=20447408; DOI=10.1016/j.jmb.2010.04.058;
RA Harmer N.J.;
RT "The structure of sedoheptulose-7-phosphate isomerase from Burkholderia
RT pseudomallei reveals a zinc binding site at the heart of the active site.";
RL J. Mol. Biol. 400:379-392(2010).
CC -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in
CC D-glycero-D-manno-heptose 7-phosphate. {ECO:0000269|PubMed:20447408}.
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 Evidence={ECO:0000269|PubMed:20447408};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:20447408};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:20447408};
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: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20447408}.
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.
CC -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily. {ECO:0000305}.
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DR EMBL; AF228583; AAK49808.1; -; Genomic_DNA.
DR EMBL; BX571965; CAH36804.1; -; Genomic_DNA.
DR RefSeq; WP_011205222.1; NC_006350.1.
DR RefSeq; YP_109390.1; NC_006350.1.
DR PDB; 2X3Y; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-197.
DR PDB; 2XBL; X-ray; 1.62 A; A/B/C/D=1-197.
DR PDB; 5LTZ; X-ray; 1.67 A; A/B/C/D=1-197.
DR PDB; 5LU5; X-ray; 1.55 A; A/B/C/D=1-197.
DR PDB; 5LU6; X-ray; 1.67 A; A/B/C/D=1-196.
DR PDB; 5LU7; X-ray; 1.92 A; A/B/C/D=1-197.
DR PDBsum; 2X3Y; -.
DR PDBsum; 2XBL; -.
DR PDBsum; 5LTZ; -.
DR PDBsum; 5LU5; -.
DR PDBsum; 5LU6; -.
DR PDBsum; 5LU7; -.
DR AlphaFoldDB; Q93UJ2; -.
DR SMR; Q93UJ2; -.
DR STRING; 272560.BPSL2795; -.
DR EnsemblBacteria; CAH36804; CAH36804; BPSL2795.
DR KEGG; bps:BPSL2795; -.
DR PATRIC; fig|272560.51.peg.2513; -.
DR eggNOG; COG0279; Bacteria.
DR OMA; TAHSNDY; -.
DR BRENDA; 5.3.1.28; 1031.
DR UniPathway; UPA00041; UER00436.
DR UniPathway; UPA00934; -.
DR EvolutionaryTrace; Q93UJ2; -.
DR Proteomes; UP000000605; 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:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:2001061; P:D-glycero-D-manno-heptose 7-phosphate 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 PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsule biogenesis/degradation; Carbohydrate metabolism;
KW Cytoplasm; Isomerase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..197
FT /note="Phosphoheptose isomerase"
FT /id="PRO_0000136521"
FT DOMAIN 40..197
FT /note="SIS"
FT BINDING 55..57
FT /ligand="substrate"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20447408"
FT BINDING 68
FT /ligand="substrate"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20447408"
FT BINDING 97..98
FT /ligand="substrate"
FT BINDING 123..125
FT /ligand="substrate"
FT BINDING 128
FT /ligand="substrate"
FT BINDING 175
FT /ligand="substrate"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20447408"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20447408"
FT MUTAGEN 61
FT /note="D->A: Less than 6% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:20447408"
FT MUTAGEN 64
FT /note="H->Q: Less than 10% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:20447408"
FT MUTAGEN 68
FT /note="E->Q: No activity."
FT /evidence="ECO:0000269|PubMed:20447408"
FT MUTAGEN 98
FT /note="D->N: No activity."
FT /evidence="ECO:0000269|PubMed:20447408"
FT MUTAGEN 124
FT /note="T->A: No activity."
FT /evidence="ECO:0000269|PubMed:20447408"
FT MUTAGEN 175
FT /note="Q->E: No activity."
FT /evidence="ECO:0000269|PubMed:20447408"
FT CONFLICT 34
FT /note="R -> Q (in Ref. 1; AAK49808)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="E -> K (in Ref. 1; AAK49808)"
FT /evidence="ECO:0000305"
FT HELIX 4..24
FT /evidence="ECO:0007829|PDB:5LU5"
FT HELIX 27..45
FT /evidence="ECO:0007829|PDB:5LU5"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:5LU5"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:5LU5"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5LU5"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5LU5"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:5LU5"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5LU5"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:5LU5"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:5LU5"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:5LU5"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:5LU5"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:5LU5"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:5LU5"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:5LU5"
FT HELIX 171..194
FT /evidence="ECO:0007829|PDB:5LU5"
SQ SEQUENCE 197 AA; 20813 MW; 22A249C834AC585B CRC64;
MENRELTYIT NSIAEAQRVM AAMLADERLL ATVRKVADAC IASIAQGGKV LLAGNGGSAA
DAQHIAGEFV SRFAFDRPGL PAVALTTDTS ILTAIGNDYG YEKLFSRQVQ ALGNEGDVLI
GYSTSGKSPN ILAAFREAKA KGMTCVGFTG NRGGEMRELC DLLLEVPSAD TPKIQEGHLV
LGHIVCGLVE HSIFGKQ
