ID A0A927JE65_9ACTN Unreviewed; 556 AA. AC A0A927JE65; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 13-SEP-2023, 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 ECO:0000313|EMBL:MBD8507391.1}; GN ORFNames=HT102_12955 {ECO:0000313|EMBL:MBD8507391.1}; OS Lolliginicoccus lacisalsi. OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae; OC Lolliginicoccus. OX NCBI_TaxID=2742202 {ECO:0000313|EMBL:MBD8507391.1, ECO:0000313|Proteomes:UP000642993}; RN [1] {ECO:0000313|EMBL:MBD8507391.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=G463 {ECO:0000313|EMBL:MBD8507391.1}; RA Yang Q., Guo P.Y., Liu S.W., Li F.N., Sun C.H.; RT "Hoyosella lacisalsi sp. nov., a halotolerant actinobacterium isolated from RT soil of Lake Gudzhirganskoe."; RL Submitted (SEP-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 -!- 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:MBD8507391.1}. 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; JACYWE010000008; MBD8507391.1; -; Genomic_DNA. DR Proteomes; UP000642993; Unassembled WGS sequence. 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 Gene3D; 6.10.250.620; -; 1. DR Gene3D; 3.20.20.540; Radical SAM ThiC family, central domain; 1. DR HAMAP; MF_00089; ThiC; 1. DR InterPro; IPR037509; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR038521; ThiC/Bza_core_dom. DR InterPro; IPR002817; ThiC/BzaA/B. DR NCBIfam; TIGR00190; thiC; 1. DR PANTHER; PTHR30557:SF1; PHOSPHOMETHYLPYRIMIDINE SYNTHASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR30557; THIAMINE BIOSYNTHESIS PROTEIN THIC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF01964; ThiC_Rad_SAM; 1. DR SFLD; SFLDF00407; phosphomethylpyrimidine_syntha; 1. DR SFLD; SFLDG01114; phosphomethylpyrimidine_syntha; 1. DR SFLD; SFLDS00113; Radical_SAM_Phosphomethylpyrim; 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}; Reference proteome {ECO:0000313|Proteomes:UP000642993}; 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 19..80 FT /note="ThiC-associated" FT /evidence="ECO:0000259|Pfam:PF13667" FT BINDING 154 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 183 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 212 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 248 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 268..270 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 309..312 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 348 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 352 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 375 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 416 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 496 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 499 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 504 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" SQ SEQUENCE 556 AA; 61241 MW; 6CCCF13B57F7B914 CRC64; MTLSSVHNPA EQAITTGPIS GSSKIYVEVP GAPGLRVPMR RVHLTNGEHL DLYDTSGPYT DTSATIDIEQ GLPRARDSWT KPAPIDGAST QLAWARAGII TDEMRFTAAR ESVSPELVRD EVARGRAVIC ANHKHPEIEP MIIGKAFSVK INGNIGNSAV TSSIGEEVEK MVWATRWGAD TIMDLSTGKN IHETREWILR SSPVPVGTVP IYQALEKVKG DPTKLNWEIY RETIIEQCEQ GVDYMTVHAG VLLRYIPLTA KRVTGIVSRG GSIMAAWCLA HHQESFLYTH FRELCEIFRE YDVTFSLGDG LRPGSIADAN DDAQFAELRT LGELTTIAKS HGVQVMIEGP GHVPMHKIVE NVRLEEELCE EAPFYTLGPL ATDIAPAYDH ITSAIGAAII AKAGTAMLCY VTPKEHPGLP NRDDVKQGVI AYKIAAHSAD LAKGHPRAQE RDDALSRARF EFRWTDQFNL SLDPDPAREY HDETLPAEPA KTAHFCSMCG PKFCSMRISA DVREYAERNG MNTQEDIDRV LAQGMAEKSA EFADHGNQVY LPLTTN //