GMHA_SHEDO
ID GMHA_SHEDO Reviewed; 196 AA.
AC Q12SK9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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}; OrderedLocusNames=Sden_0271;
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000255|HAMAP-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 -!- 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; CP000302; ABE53567.1; -; Genomic_DNA.
DR RefSeq; WP_011494734.1; NC_007954.1.
DR AlphaFoldDB; Q12SK9; -.
DR SMR; Q12SK9; -.
DR STRING; 318161.Sden_0271; -.
DR EnsemblBacteria; ABE53567; ABE53567; Sden_0271.
DR KEGG; sdn:Sden_0271; -.
DR eggNOG; COG0279; Bacteria.
DR HOGENOM; CLU_080999_3_1_6; -.
DR OMA; DVHICVP; -.
DR OrthoDB; 1571626at2; -.
DR UniPathway; UPA00041; UER00436.
DR Proteomes; UP000001982; Chromosome.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Isomerase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..196
FT /note="Phosphoheptose isomerase"
FT /id="PRO_1000197017"
FT DOMAIN 34..196
FT /note="SIS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 49..51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 91..92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 117..119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
SQ SEQUENCE 196 AA; 20871 MW; B3B54D5B41CFED1B CRC64;
MLERIKDSFT ESIQTKIDAA EALPESIEKA AEMMVQCLLG GKKILACGNG GSAGDAQHFS
AELLNRYEIE RPPLPAIALS TDTSTITAIA NDYSYDEIFS KQIFALGQPG DILLAISTSG
NSGNIIKAME AALSRDMTIV ALTGKDGGAM AGLMSAGDVE IRVPSNVTAR IQEVHLLVIH
CLCDNIDRTL FPQDEA
