ID A0A3M5S4U8_PSEAV Unreviewed; 198 AA. AC A0A3M5S4U8; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 02-JUN-2021, entry version 8. DE RecName: Full=Phosphoheptose isomerase {ECO:0000256|HAMAP-Rule:MF_00067}; DE EC=5.3.1.28 {ECO:0000256|HAMAP-Rule:MF_00067}; DE AltName: Full=Sedoheptulose 7-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00067}; GN Name=gmhA {ECO:0000256|HAMAP-Rule:MF_00067}; GN ORFNames=ALP54_00250 {ECO:0000313|EMBL:RMT09687.1}, ALQ79_02830 GN {ECO:0000313|EMBL:RMM50776.1}; OS Pseudomonas amygdali pv. lachrymans (Pseudomonas syringae pv. lachrymans). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali. OX NCBI_TaxID=53707 {ECO:0000313|EMBL:RMT09687.1, ECO:0000313|Proteomes:UP000274764}; RN [1] {ECO:0000313|Proteomes:UP000270105, ECO:0000313|Proteomes:UP000274764} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N7512 {ECO:0000313|EMBL:RMT09687.1, RC ECO:0000313|Proteomes:UP000274764}, and YM8003 RC {ECO:0000313|EMBL:RMM50776.1, ECO:0000313|Proteomes:UP000270105}; RA Dillon M., Thakur S., Almeida R.N.D., Weir B.S., Guttman D.S.; RT "Recombination of ecologically and evolutionarily significant loci RT maintains genetic cohesion in the Pseudomonas syringae species complex."; RL Submitted (AUG-2018) 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:0000256|ARBA:ARBA00003172, CC ECO:0000256|HAMAP-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; CC Evidence={ECO:0000256|ARBA:ARBA00000348, ECO:0000256|HAMAP- CC Rule:MF_00067}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00067}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00067}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00067}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|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:0000256|HAMAP-Rule:MF_00067}. CC -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily. CC {ECO:0000256|ARBA:ARBA00009894, ECO:0000256|HAMAP-Rule:MF_00067}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RMT09687.1}. 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; RBOH01000031; RMM50776.1; -; Genomic_DNA. DR EMBL; RBTB01000194; RMT09687.1; -; Genomic_DNA. DR EnsemblBacteria; RMM50776; RMM50776; ALQ79_02830. DR EnsemblBacteria; RMT09687; RMT09687; ALP54_00250. DR UniPathway; UPA00041; UER00436. DR Proteomes; UP000270105; Unassembled WGS sequence. DR Proteomes; UP000274764; Unassembled WGS sequence. 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. DR Pfam; PF13580; SIS_2; 1. DR PROSITE; PS51464; SIS; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP- KW Rule:MF_00067}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00067}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00067}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00067}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00067}. FT DOMAIN 37..198 FT /note="SIS" FT /evidence="ECO:0000259|PROSITE:PS51464" FT REGION 52..54 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT REGION 94..95 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT REGION 120..122 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT METAL 61 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT METAL 65 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT METAL 175 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT METAL 183 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT BINDING 65 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT BINDING 125 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT BINDING 175 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" SQ SEQUENCE 198 AA; 21476 MW; 093DA55983F7D521 CRC64; MMDMQSRIRR LFQASIETKQ QSMEVLAPYI EQASQVMVNA LLNEGKMLAC GNGGSAGDAQ HFSSELLNRF ERERPSLPAI ALTTDSSTIT SIANDYSYNE IFSKQIRALG QPGDVLLAIS TSGNSANIIQ AIQAAHDREM IVVALTGRDG GGMASLLLPE DVEIRVPANV TARIQEVHLL AIHCLCDLID SQLFGSEE //