ID   GMHA_BURMA              Reviewed;         197 AA.
AC   Q9AI36; Q62HG3;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   28-JAN-2026, entry version 115.
DE   RecName: Full=Phosphoheptose isomerase {ECO:0000255|HAMAP-Rule:MF_00067};
DE            EC=5.3.1.28 {ECO:0000255|HAMAP-Rule:MF_00067};
DE   AltName: Full=Sedoheptulose 7-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00067};
GN   Name=gmhA {ECO:0000255|HAMAP-Rule:MF_00067};
GN   OrderedLocusNames=BMA2295;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=11373120; DOI=10.1006/mpat.2000.0430;
RA   DeShazer D., Waag D.M., Fritz D.L., Woods D.E.;
RT   "Identification of a Burkholderia mallei polysaccharide gene cluster by
RT   subtractive hybridization and demonstration that the encoded capsule is an
RT   essential virulence determinant.";
RL   Microb. Pathog. 30:253-269(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(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).
CC   -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in
CC       D-glycero-D-manno-heptose 7-phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_00067}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00067};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00067};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00067};
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. {ECO:0000255|HAMAP-Rule:MF_00067}.
CC   -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00067}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00067}.
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:0000255|HAMAP-Rule:MF_00067}.
CC   -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00067}.
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DR   EMBL; AF285636; AAK26468.1; -; Genomic_DNA.
DR   EMBL; CP000010; AAU49838.1; -; Genomic_DNA.
DR   RefSeq; WP_004194315.1; NC_006348.1.
DR   AlphaFoldDB; Q9AI36; -.
DR   SMR; Q9AI36; -.
DR   GeneID; 93061384; -.
DR   KEGG; bma:BMA2295; -.
DR   PATRIC; fig|243160.12.peg.2362; -.
DR   eggNOG; COG0279; Bacteria.
DR   HOGENOM; CLU_080999_0_1_4; -.
DR   BRENDA; 5.3.1.28; 1030.
DR   UniPathway; UPA00041; UER00436.
DR   UniPathway; UPA00934; -.
DR   Proteomes; UP000006693; 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   Gene3D; 3.40.50.10490; Glucose-6-phosphate isomerase like protein, domain 1; 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   InterPro; IPR050099; SIS_GmhA/DiaA_subfam.
DR   PANTHER; PTHR30390:SF6; DNAA INITIATOR-ASSOCIATING PROTEIN DIAA; 1.
DR   PANTHER; PTHR30390; SEDOHEPTULOSE 7-PHOSPHATE ISOMERASE / DNAA INITIATOR-ASSOCIATING FACTOR FOR REPLICATION INITIATION; 1.
DR   Pfam; PF13580; SIS_2; 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Carbohydrate metabolism; Cytoplasm;
KW   Isomerase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..197
FT                   /note="Phosphoheptose isomerase"
FT                   /id="PRO_0000136520"
FT   DOMAIN          40..197
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         55..57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         97..98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         123..125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   CONFLICT        26
FT                   /note="D -> N (in Ref. 1; AAK26468)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   197 AA;  20784 MW;  63A1B00CA5E440D4 CRC64;
     MENRELTYIT NSIAEAQRVM AAMLADERLL ATVQKVADAC IASIAQGGKV LLAGNGGSAA
     DAQHIAGEFV SRFAFDRPGL PAVALTTDTS ILTAIGNDYG YEKLFSRQVQ ALGNKGDVLI
     GYSTSGKSPN ILAAFREAKA KGMTCVGFTG NRGGEMRELC DLLLEVPSAD TPKIQEGHLV
     LGHIVCGLVE HSIFGKQ
//