ID GMHA_AERHH Reviewed; 192 AA. AC A0KIK9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 97. 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=AHA_1574; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / RC KCTC 2358 / NCIMB 9240 / NCTC 8049; RX PubMed=16980456; DOI=10.1128/jb.00621-06; RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.; RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."; RL J. Bacteriol. 188:8272-8282(2006). 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000462; ABK36369.1; -; Genomic_DNA. DR RefSeq; WP_011705469.1; NC_008570.1. DR RefSeq; YP_856110.1; NC_008570.1. DR AlphaFoldDB; A0KIK9; -. DR SMR; A0KIK9; -. DR STRING; 380703.AHA_1574; -. DR EnsemblBacteria; ABK36369; ABK36369; AHA_1574. DR GeneID; 77274836; -. DR KEGG; aha:AHA_1574; -. DR PATRIC; fig|380703.7.peg.1585; -. DR eggNOG; COG0279; Bacteria. DR HOGENOM; CLU_080999_4_0_6; -. DR OrthoDB; 9810929at2; -. DR UniPathway; UPA00041; UER00436. DR Proteomes; UP000000756; 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 NCBIfam; TIGR00441; gmhA; 1. DR PANTHER; PTHR30390:SF7; PHOSPHOHEPTOSE ISOMERASE; 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 Carbohydrate metabolism; Cytoplasm; Isomerase; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1..192 FT /note="Phosphoheptose isomerase" FT /id="PRO_1000009047" FT DOMAIN 37..192 FT /note="SIS" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067" FT BINDING 52..54 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067" FT BINDING 65 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067" FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067" FT BINDING 93..94 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067" FT BINDING 119..121 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067" FT BINDING 124 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 192 AA; 20868 MW; DDE30BA4C885CA57 CRC64; MYQELIRNEL TEAASVLQAF LADEQNLKDI EAAAKLLADS FKQEGKVLSC GNGGSHCDAM HFAEELTGRY RENRPGYAGI AISDPSHLSC VSNDFGYDYV FSRYVEAVGR RGDVLLGIST SGNSGNILKA IEAAHAKGMK VIALTGKDGG KMAGLADVEI RVPHFGYADR IQEVHIKVIH ILIQLVEKEM AK //