位置:首页 > 蛋白库 > THIC_COXBU
THIC_COXBU
ID   THIC_COXBU              Reviewed;         554 AA.
AC   Q83EJ0;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 100.
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=CBU_0330;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00089}.
CC   -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00089}.
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; AE016828; AAO89886.2; -; Genomic_DNA.
DR   RefSeq; NP_819372.2; NC_002971.3.
DR   AlphaFoldDB; Q83EJ0; -.
DR   SMR; Q83EJ0; -.
DR   STRING; 227377.CBU_0330; -.
DR   EnsemblBacteria; AAO89886; AAO89886; CBU_0330.
DR   GeneID; 1208212; -.
DR   KEGG; cbu:CBU_0330; -.
DR   PATRIC; fig|227377.7.peg.324; -.
DR   eggNOG; COG0422; Bacteria.
DR   HOGENOM; CLU_013181_2_1_6; -.
DR   OMA; TWELFRD; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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; IPR025747; ThiC-associated_dom.
DR   InterPro; IPR038521; ThiC/Bza_core_dom.
DR   InterPro; IPR002817; ThiC/BzaA/B.
DR   PANTHER; PTHR30557; PTHR30557; 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;
KW   4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome;
KW   S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc.
FT   CHAIN           1..554
FT                   /note="Phosphomethylpyrimidine synthase"
FT                   /id="PRO_0000152802"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         302..304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         343..346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         382
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         386
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         409
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         450
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         530
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         533
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         538
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   554 AA;  62594 MW;  CBBC713DBDFE7784 CRC64;
     MRREGTMRLH RTFLLRVYLK ESAVITYPAS KKIYCQGKIF PTIRVGMREI QLTNGDSLTL
     YDTSGPYSDP NISIKSPQGL PRLREPWIKV RPRKTQLAFA KEGVITPEME YAAIRENQKR
     ELKKNTDQER ERRLQGNSLS ARIPNPITPE FIRNEIACGR AILPANINHP ESEPMIIGRH
     FLVKVNANIG NSSLTSSVEE EVEKLIWALR WGADTVMDLS TGKKIKEIRE TILRHSPVPI
     GTVPLYEALE KVDGDVKALT WEIFRDTLIS QAEQGVDYFT IHAGVLNRFI PLTQKRVTGI
     VSRGGSLMAK WCLLHREENF LYTHFTEICE IMRAYDVSFS LGDGLRPGSI ADANDEAQFA
     ELKIQGELNR IAWKYGVQVM NEGPGHIPLN LIEENMTKQL AYCREAPFYT LGPLTTDIAP
     GYDHIGSAIG AAFIAWQGCA LLCYVTPKEH LGLPNKQDVK EGLIAYKIAA HAADLAKGHP
     AARQRDYLLS QARFEFRWHD QFNLALDAET ARLFHDETLP KEAAKHAHFC SLCGPKFCAY
     KTSHEVRDTL QKVT
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024