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THIC_CLOP1
ID   THIC_CLOP1              Reviewed;         436 AA.
AC   Q0TTB7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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}; OrderedLocusNames=CPF_0670;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC   Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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:0000255|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: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 coordinated
CC       with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000255|HAMAP-Rule:MF_00089};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00089}.
CC   -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00089}.
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DR   EMBL; CP000246; ABG82595.1; -; Genomic_DNA.
DR   RefSeq; WP_003456962.1; NC_008261.1.
DR   AlphaFoldDB; Q0TTB7; -.
DR   SMR; Q0TTB7; -.
DR   STRING; 195103.CPF_0670; -.
DR   PRIDE; Q0TTB7; -.
DR   EnsemblBacteria; ABG82595; ABG82595; CPF_0670.
DR   GeneID; 29572206; -.
DR   KEGG; cpf:CPF_0670; -.
DR   eggNOG; COG0422; Bacteria.
DR   HOGENOM; CLU_013181_2_2_9; -.
DR   OMA; TWELFRD; -.
DR   OrthoDB; 505395at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001823; Chromosome.
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; IPR038521; ThiC/Bza_core_dom.
DR   InterPro; IPR002817; ThiC/BzaA/B.
DR   PANTHER; PTHR30557; PTHR30557; 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; Iron; Iron-sulfur; Lyase; Metal-binding; S-adenosyl-L-methionine;
KW   Thiamine biosynthesis; Zinc.
FT   CHAIN           1..436
FT                   /note="Phosphomethylpyrimidine synthase"
FT                   /id="PRO_1000004754"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         185..187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         226..229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         409
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         412
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         416
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
SQ   SEQUENCE   436 AA;  48718 MW;  3BCFE593E9DA0C55 CRC64;
     MNYTTQMDAA KKGIITKEMQ VVSEKEGINI ETLMNLMAEG KIVIPANKNH KSISAEGVGQ
     GLRTKINVNL GISKDCANIE LELEKVKKAI DMNAESIMDL SNYGKTYDFR KRLVEVSTAM
     IGTVPMYDVV GFYDKELKDI TVDEFFEVVE KHAKDGVDFV TIHAGLNRET IETFRRNKRL
     TNIVSRGGSL LFAWMELNNR ENPFYEYFDR LLDICEKYDL TLSLGDACRP GSIADATDAV
     QIKELITLGE LTKRAWERNV QVIIEGPGHM AMNEIEANVL LEKKLCHGAP FYVLGPIVTD
     IAPGYDHITS AIGGAMAASY GADFLCYVTP AEHLRLPNLE DVREGIVATK IAAHAADIAK
     GISGARDIDN KMSDARKRLD WDEMFSLAID SEKAIRYRKE STPEHKDSCT MCGKMCSIRN
     MNKILEGKDI NLLRED
 
 
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