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   14-MAY-2014, entry version 59.
DE   RecName: Full=Phosphomethylpyrimidine synthase;
DE            EC=4.1.99.17;
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].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S.1;
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 + formate + CO.
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   -!- SIMILARITY: Belongs to the ThiC family.
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DR   EMBL; CP000230; ABC22808.1; -; Genomic_DNA.
DR   RefSeq; YP_427095.1; NC_007643.1.
DR   ProteinModelPortal; Q2RST7; -.
DR   STRING; 269796.Rru_A2008; -.
DR   EnsemblBacteria; ABC22808; ABC22808; Rru_A2008.
DR   GeneID; 3835433; -.
DR   KEGG; rru:Rru_A2008; -.
DR   PATRIC; 23327690; VBIRhoRub82919_2092.
DR   eggNOG; COG0422; -.
DR   HOGENOM; HOG000224484; -.
DR   KO; K03147; -.
DR   OMA; NTANESA; -.
DR   OrthoDB; EOG6NWBM5; -.
DR   BioCyc; RRUB269796:GCN1-2041-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00089; ThiC; 1.
DR   InterPro; IPR002817; ThiC.
DR   InterPro; IPR025747; ThiC-associated_dom.
DR   Pfam; PF01964; ThiC; 1.
DR   Pfam; PF13667; ThiC-associated; 1.
DR   TIGRFAMs; TIGR00190; thiC; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding;
KW   Reference proteome; S-adenosyl-L-methionine; Thiamine biosynthesis;
KW   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
//