ID GMHA_PROMH Reviewed; 192 AA. AC B4EUT1; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 88. 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=PMI0349; OS Proteus mirabilis (strain HI4320). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Proteus. OX NCBI_TaxID=529507; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI4320; RX PubMed=18375554; DOI=10.1128/jb.01981-07; RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N., RA Parkhill J., Mobley H.L.T.; RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of RT both adherence and motility."; RL J. Bacteriol. 190:4027-4037(2008). 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; AM942759; CAR40905.1; -; Genomic_DNA. DR RefSeq; WP_004244807.1; NC_010554.1. DR AlphaFoldDB; B4EUT1; -. DR SMR; B4EUT1; -. DR EnsemblBacteria; CAR40905; CAR40905; PMI0349. DR GeneID; 6800936; -. DR KEGG; pmr:PMI0349; -. DR eggNOG; COG0279; Bacteria. DR HOGENOM; CLU_080999_4_0_6; -. DR UniPathway; UPA00041; UER00436. DR Proteomes; UP000008319; 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; Zinc. FT CHAIN 1..192 FT /note="Phosphoheptose isomerase" FT /id="PRO_1000092284" 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; 20852 MW; 93C044E549B39254 CRC64; MYQDLIRGEL TEAADTLSRF LQDDANIEAI QKAAVLLADS FKAGGKVLSC GNGGSHCDAM HFAEELTGRY RENRPGYPAI AISDVSHISC VSNDFGYEYV FSRYVEAVGK EGDVLLGIST SGNSGNIIKA ISAAREKGMK VITLTGKDGG KMAGSADIEI RVPHFGYADR IQEIHIKVIH ILIQLIEKEM EK //