(data stored in ACNUC7421 zone)

SWISSPROT: THIC_PSEHT

ID   THIC_PSEHT              Reviewed;         650 AA.
AC   Q3IFN9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 78.
DE   RecName: Full=Phosphomethylpyrimidine synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE            EC=4.1.99.17 {ECO:0000255|HAMAP-Rule:MF_00089};
DE   AltName: Full=Hydroxymethylpyrimidine phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE            Short=HMP-P synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE            Short=HMP-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE            Short=HMPP synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE   AltName: Full=Thiamine biosynthesis protein ThiC {ECO:0000255|HAMAP-Rule:MF_00089};
GN   Name=thiC {ECO:0000255|HAMAP-Rule:MF_00089};
GN   OrderedLocusNames=PSHAa0480;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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. {ECO:0000255|HAMAP-Rule:MF_00089}.
CC   -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-
CC       adenosyl-L-methionine = 4-amino-2-methyl-5-
CC       (phosphomethyl)pyrimidine + 5'-deoxyadenosine + L-methionine +
CC       formate + CO. {ECO:0000255|HAMAP-Rule:MF_00089}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00089};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is
CC       coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC       methionine. {ECO:0000255|HAMAP-Rule:MF_00089};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00089}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00089}.
CC   -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00089}.
DR   EMBL; CR954246; CAI85576.1; -; Genomic_DNA.
DR   RefSeq; WP_011327189.1; NC_007481.1.
DR   ProteinModelPortal; Q3IFN9; -.
DR   SMR; Q3IFN9; -.
DR   STRING; 326442.PSHAa0480; -.
DR   EnsemblBacteria; CAI85576; CAI85576; PSHAa0480.
DR   KEGG; pha:PSHAa0480; -.
DR   PATRIC; fig|326442.8.peg.456; -.
DR   eggNOG; ENOG4105CBF; Bacteria.
DR   eggNOG; COG0422; LUCA.
DR   HOGENOM; HOG000224484; -.
DR   KO; K03147; -.
DR   OMA; TWELFRD; -.
DR   OrthoDB; POG091H02FB; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000006843; Chromosome I.
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:thiamine biosynthetic process; IEA:UniProtKB-KW.
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   PANTHER; PTHR30557:SF2; PTHR30557:SF2; 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;
DR   PRODOM; Q3IFN9.
DR   SWISS-2DPAGE; Q3IFN9.
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    650       Phosphomethylpyrimidine synthase.
FT                                /FTId=PRO_0000242286.
FT   REGION      355    357       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   REGION      396    399       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   METAL       439    439       Zinc. {ECO:0000255|HAMAP-Rule:MF_00089}.
FT   METAL       503    503       Zinc. {ECO:0000255|HAMAP-Rule:MF_00089}.
FT   METAL       583    583       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_00089}.
FT   METAL       586    586       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_00089}.
FT   METAL       591    591       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_00089}.
FT   BINDING     241    241       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   BINDING     270    270       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   BINDING     299    299       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   BINDING     335    335       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   BINDING     435    435       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   BINDING     462    462       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
SQ   SEQUENCE   650 AA;  73314 MW;  7054B992795A2DB8 CRC64;
     MSNTAKKSSR RETRAAASEY IYNLTGQPFP NSHKVYVEGT QNNIRVGMRE ITLSDTYIGG
     SDENPVYEPN EPLRVYDTSG PYTDPNFKLD VRQGLAKFRE QWIESRGDTE LLESVTSRFT
     QQRMADEGLD HLRFEHLPKI RRGKAGKNVT QMHYARQGII TPEMEYVAIR ENMGRKKIHA
     ELLAAQHKGE SFGASIPDFI TPEFVRDEIA RGRAILPNNI NHPETEPMIV GRNFLVKVNA
     NIGNSSVSSS IEEEVEKMVW STRWGADTVM DLSTGRYIHE TREWVVRNSP VPIGTVPIYQ
     ALEKVNGVAE DLTWEIFRDT LIEQAEQGVD YFTIHAGVLL RYVPMTAKRV TGIVSRGGSI
     MAKWCLAHHK ENFLYTHFED ICEILKQYDI CFSLGDGLRP GSIADANDEA QFSELRTLGE
     LTKLAWKHDV QVFIEGPGHV PMHMIKANMD EQLKHCDEAP FYTLGPLTTD IAPGYDHITS
     GIGAAQIAWY GCAMLCYVTP KEHLGLPNKE DVKEGLITYK IAAHAADLAK GHPGAQERDN
     ALSKARFEFR WHDQFNIGLD PERAREYHDE TLPQESGKVA HFCSMCGPKF CSMKISQEVR
     EYAKDLEARG IDPANAADTI TIKMIDVEAQ MKAKSDEFKK TGSEIYHKAI
//

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