ID Q3STR1_NITWN Unreviewed; 197 AA. AC Q3STR1; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 04-NOV-2026, entry version 125. 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 OrderedLocusNames=Nwi_1068 {ECO:0000313|EMBL:ABA04330.1}; OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 / OS NCIMB 11846 / Nb-255). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Nitrobacteraceae; Nitrobacter. OX NCBI_TaxID=323098 {ECO:0000313|EMBL:ABA04330.1, ECO:0000313|Proteomes:UP000002531}; RN [1] {ECO:0000313|EMBL:ABA04330.1, ECO:0000313|Proteomes:UP000002531} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255 RC {ECO:0000313|Proteomes:UP000002531}; RX PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006; RA Starkenburg S.R., Chain P.S., Sayavedra-Soto L.A., Hauser L., Land M.L., RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., RA Hickey W.J.; RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium RT Nitrobacter winogradskyi Nb-255."; RL Appl. Environ. Microbiol. 72:2050-2063(2006). 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; Evidence={ECO:0000256|HAMAP- CC 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 --------------------------------------------------------------------------- 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; CP000115; ABA04330.1; -; Genomic_DNA. DR RefSeq; WP_011314364.1; NC_007406.1. DR AlphaFoldDB; Q3STR1; -. DR STRING; 323098.Nwi_1068; -. DR KEGG; nwi:Nwi_1068; -. DR eggNOG; COG0279; Bacteria. DR HOGENOM; CLU_080999_4_0_5; -. DR OMA; AACHVQE; -. DR OrthoDB; 9810929at2; -. DR UniPathway; UPA00041; UER00436. DR Proteomes; UP000002531; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-UniRule. 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 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000002531}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00067}. FT DOMAIN 37..196 FT /note="SIS" FT /evidence="ECO:0000259|PROSITE:PS51464" FT BINDING 52..54 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT BINDING 65 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT BINDING 94..95 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT BINDING 120..122 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT BINDING 125 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT BINDING 172 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT BINDING 172 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" FT BINDING 180 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067" SQ SEQUENCE 197 AA; 20743 MW; D62CE7B3B245414C CRC64; MSQNPIAVHF QQSLAALQRA ANDTTLLAAA SEIAVTIIDA LRSGNKVLLI GNGGSAADAQ HIASEIVGRY RKERPGYAAI ALTTDTSALT AISNDYGFER IFCRQIESLG RPGDILLALS TSGRSPNILT ALDAARRLGL VTAGFTGLKG QSLREVCDHL LVAPSDDTPV IQQIHMTAAH AICDTVEHAL ADGDSDR //