ID A0A6J4K6D7_9BACT Unreviewed; 574 AA. AC A0A6J4K6D7; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 07-APR-2021, entry version 4. DE RecName: Full=Phosphomethylpyrimidine synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE EC=4.1.99.17 {ECO:0000256|HAMAP-Rule:MF_00089}; DE AltName: Full=Hydroxymethylpyrimidine phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE Short=HMP-P synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE Short=HMP-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE Short=HMPP synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE AltName: Full=Thiamine biosynthesis protein ThiC {ECO:0000256|HAMAP-Rule:MF_00089}; GN Name=thiC {ECO:0000256|HAMAP-Rule:MF_00089}; GN ORFNames=AVDCRST_MAG68-67 {ECO:0000313|EMBL:CAA9296999.1}; OS uncultured Gemmatimonadetes bacterium. OC Bacteria; Gemmatimonadetes; environmental samples. OX NCBI_TaxID=203437 {ECO:0000313|EMBL:CAA9296999.1}; RN [1] {ECO:0000313|EMBL:CAA9296999.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AVDCRST_MAG68 {ECO:0000313|EMBL:CAA9296999.1}; RA Meier V. D.; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) CC in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. CC {ECO:0000256|ARBA:ARBA00003175, ECO:0000256|HAMAP-Rule:MF_00089}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L- CC methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'- CC deoxyadenosine + CO + formate + 3 H(+) + L-methionine; CC Xref=Rhea:RHEA:24840, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, CC ChEBI:CHEBI:17245, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844, CC ChEBI:CHEBI:58354, ChEBI:CHEBI:59789, ChEBI:CHEBI:137981; CC EC=4.1.99.17; Evidence={ECO:0000256|HAMAP-Rule:MF_00089}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00089}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|HAMAP-Rule:MF_00089}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00089}. CC -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000256|HAMAP- CC Rule:MF_00089}. 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; CADCTW010000007; CAA9296999.1; -; Genomic_DNA. DR UniPathway; UPA00060; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.540; -; 1. DR HAMAP; MF_00089; ThiC; 1. DR InterPro; IPR037509; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR038521; ThiC/Bza_sf. DR InterPro; IPR002817; ThiC/BzaA/B. DR PANTHER; PTHR30557; PTHR30557; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF01964; ThiC_Rad_SAM; 1. DR SFLD; SFLDF00407; phosphomethylpyrimidine_syntha; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00089}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00089}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_00089}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00089}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00089}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_00089}; KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP- KW Rule:MF_00089}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00089}. FT DOMAIN 21..82 FT /note="ThiC-associated" FT /evidence="ECO:0000259|Pfam:PF13667" FT REGION 294..296 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT REGION 335..338 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT METAL 378 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT METAL 442 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT METAL 522 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT METAL 525 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT METAL 530 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 180 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 209 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 238 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 274 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 374 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 401 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" SQ SEQUENCE 574 AA; 64015 MW; E9E33A55B715E728 CRC64; MTNGERGTRN GERAGDYGDN FPASRKVYVD GRHGVRVPMR EIVLSGGEPP LRVYDTSGPL GGDVRRGLEP LRAEWIRARG DVAEAARTYR PLPGAQVVEM PEALHRPTLR GTGCVTQMAY ARRGEITAEM EFVALREGMS PEFVRDEVAR GRAIIPANIN HPELEPMIIG RGFKVKVNAN IGNSAVTSSI EEEVEKLRWA TLWGADTVMD LSTGKNIHET REWILRNSPV PIGTVPIYQA LEKVGGVPEE LTWELYRDTL IEQAEQGVDY FTVHAGVLLR YVPMTANRLT GIVSRGGSII AKWCLAHHRE SFLYTHFREI CEIMRAYDVS FSLGDGLRPG SIRDANDEAQ FAELRTQGEL NRIAWEFDVQ TMNEGPGHVP MHLIQENMDR QLEWCHEAPF YTLGPLTTDI APGYDHITSA IGAAQIGWYG TAMLCYVTPK EHLGLPNRDD VKAGVITYKI AAHAADLAKR HPRAQEWDDA LSKARFEFRW RDQFNLSLDP VTALSYHDET LPAEGAKIAH FCSMCGPKFC SMKITQDVRD YAAKQAAAEA GMAEKSVEFR EKGAEIYLPE PAVP //