ID Q1MPL3_LAWIP Unreviewed; 211 AA. AC Q1MPL3; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 02-APR-2025, entry version 104. 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 ECO:0000313|EMBL:CAJ55064.1}; GN OrderedLocusNames=LI1010 {ECO:0000313|EMBL:CAJ55064.1}; OS Lawsonia intracellularis (strain PHE/MN1-00). OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia; OC Desulfovibrionales; Desulfovibrionaceae; Lawsonia. OX NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ55064.1, ECO:0000313|Proteomes:UP000002430}; RN [1] {ECO:0000313|EMBL:CAJ55064.1, ECO:0000313|Proteomes:UP000002430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ55064.1, RC ECO:0000313|Proteomes:UP000002430}; RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L., RA Peterson A., May B., Singh S., Gebhart C., Kapur V.; RT "The complete genome sequence of Lawsonia intracellularis: the causative RT agent of proliferative enteropathy."; RL Submitted (NOV-2005) 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|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; 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 -!- 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; AM180252; CAJ55064.1; -; Genomic_DNA. DR RefSeq; WP_011527093.1; NC_008011.1. DR AlphaFoldDB; Q1MPL3; -. DR STRING; 363253.LI1010; -. DR KEGG; lip:LI1010; -. DR eggNOG; COG0279; Bacteria. DR HOGENOM; CLU_080999_3_0_7; -. DR OrthoDB; 9810929at2; -. DR UniPathway; UPA00041; UER00436. DR Proteomes; UP000002430; 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 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; 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:UP000002430}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00067}. FT DOMAIN 37..199 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 211 AA; 22543 MW; 5238613A17113A99 CRC64; MNKAFQLITS HLETGIKLRS EFFTAHASTI VEMARQIASS VACGGKIIIA GNGGSAADAQ HWAGEFVNRF LLDRPPLPAI ALTTDSSILT AIGNDFGFHL IFAKQLQAIG QQGDVFLGIS TSGNSVNLIE ALHVARKQRI TTVGLTGKGG GGMAPLCDFL IDVPHQSTPL VQEVHATIGH MLCMLIDYFL FENVSAIQPL LNDPAPHENN E //