ID THIC_RHORT Reviewed; 621 AA. AC Q2RST7; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 30-NOV-2010, entry version 37. DE RecName: Full=Phosphomethylpyrimidine synthase; DE EC=4.-.-.-; DE AltName: Full=Hydroxymethylpyrimidine phosphate synthase; DE Short=HMP-P synthase; DE Short=HMP-phosphate synthase; DE Short=HMPP synthase; DE AltName: Full=Thiamine biosynthesis protein thiC; GN Name=thiC; OrderedLocusNames=Rru_A2008; OS Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., RA Reslewic S., Zhou S., Schwartz D.C.; RT "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC RT 11170."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction (By similarity). CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine CC + 5'-deoxyadenosine + L-methionine. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- MISCELLANEOUS: The reaction is still not fully elucidated. Not all CC reaction products are known. The shown reaction is thus not CC balanced. CC -!- SIMILARITY: Belongs to the thiC family. 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; CP000230; ABC22808.1; -; Genomic_DNA. DR RefSeq; YP_427095.1; NC_007643.1. DR STRING; Q2RST7; -. DR GeneID; 3835433; -. DR GenomeReviews; CP000230_GR; Rru_A2008. DR KEGG; rru:Rru_A2008; -. DR NMPDR; fig|1085.1.peg.2583; -. DR eggNOG; COG0422; -. DR HOGENOM; HBG285234; -. DR OMA; TWELFRD; -. DR PhylomeDB; Q2RST7; -. DR ProtClustDB; PRK09284; -. DR BioCyc; RRUB269796:RRU_A2008-MONOMER; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009228; P:thiamin biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_00089; ThiC; 1; -. DR InterPro; IPR002817; ThiC. DR Pfam; PF01964; ThiC; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. FT CHAIN 1 621 Phosphomethylpyrimidine synthase. FT /FTId=PRO_0000242298. FT REGION 329 331 Substrate binding (By similarity). FT REGION 370 373 Substrate binding (By similarity). FT METAL 413 413 Zinc (By similarity). FT METAL 477 477 Zinc (By similarity). FT METAL 557 557 Iron-sulfur (4Fe-4S-S-AdoMet) (By FT similarity). FT METAL 560 560 Iron-sulfur (4Fe-4S-S-AdoMet) (By FT similarity). FT METAL 565 565 Iron-sulfur (4Fe-4S-S-AdoMet) (By FT similarity). FT BINDING 215 215 Substrate (By similarity). FT BINDING 244 244 Substrate (By similarity). FT BINDING 273 273 Substrate (By similarity). FT BINDING 309 309 Substrate (By similarity). FT BINDING 409 409 Substrate (By similarity). FT BINDING 436 436 Substrate (By similarity). SQ SEQUENCE 621 AA; 66602 MW; 73ED29E7D7D1C7F9 CRC64; MTAPFLSSLS PTSPLASATA PFPGSRKVYA RPADAPHLRV PFREIILSDP GEAPVRVADP SGPYSDPEAT IDLRQGLARH RASWASARGN STVTAGRPAP SEGDFEAFPL TYAPLRRRDE TPFTQLEYAR AGVITDEMIY VATRENLGRD SAVAGACARL AGGEAFGAAL PAHVTPEFVR AEIAAGRAII PANINHPELE PTIIGRNFLV KVNANIGNSA LGSSIEDEVA KLVWAIRWGA DTVMDLSTGK AIHATREWIL RNSPVPIGTV PLYQALEKVG GDATRLDWAV FEDTLIEQCE QGVDYFTIHA GVRLAHIPLT ASRTTGIVSR GGSILAKWCL SHHRENFLYE RFADICAILR RYDVAFSLGD GLRPGSVADA NDAAQFAELD TLGALTAVAW EHGCQVMVEG PGHVPMHKIK ANMDRQLATC GEAPFYTLGP LTTDIAPGHD HITSAIGAAM IGWFGTAMLC YVTPKEHLGL PDRADVKAGV IAYKLAAHAA DIAKGHPAAQ LRDDAISRAR FDFRWSDQFN LGLDPEGARA FHDETLPHAA HKTAHFCSMC GPKFCSMKIS HDIRDGALEG ADALTQAGLD QMSATFRASG GEVHLDAQAL DALAWEGKPA R //