(data stored in ACNUC29543 zone)

SWISSPROT: THIC_ACIBT

ID   THIC_ACIBT              Reviewed;         625 AA.
AC   A3M1D2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAY-2019, 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=A1S_0251;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-
CC         adenosyl-L-methionine = 4-amino-2-methyl-5-
CC         (phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate
CC         + 3 H(+) + L-methionine; Xref=Rhea:RHEA:24840,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:17245,
CC         ChEBI:CHEBI:17319, ChEBI:CHEBI:57844, ChEBI:CHEBI:58354,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:137981; EC=4.1.99.17;
CC         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
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; CP000521; ABO10726.2; -; Genomic_DNA.
DR   SMR; A3M1D2; -.
DR   EnsemblBacteria; ABO10726; ABO10726; A1S_0251.
DR   KEGG; acb:A1S_0251; -.
DR   HOGENOM; HOG000224484; -.
DR   KO; K03147; -.
DR   UniPathway; UPA00060; -.
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; IPR025747; ThiC-associated_dom.
DR   InterPro; IPR038521; ThiC/Bza_sf.
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;
DR   PRODOM; A3M1D2.
DR   SWISS-2DPAGE; A3M1D2.
KW   4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding;
KW   S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc.
FT   CHAIN         1    625       Phosphomethylpyrimidine synthase.
FT                                /FTId=PRO_1000093184.
FT   REGION      345    347       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   REGION      386    389       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   METAL       429    429       Zinc. {ECO:0000255|HAMAP-Rule:MF_00089}.
FT   METAL       493    493       Zinc. {ECO:0000255|HAMAP-Rule:MF_00089}.
FT   METAL       573    573       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_00089}.
FT   METAL       576    576       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_00089}.
FT   METAL       581    581       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_00089}.
FT   BINDING     231    231       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   BINDING     260    260       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   BINDING     289    289       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   BINDING     325    325       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   BINDING     425    425       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
FT   BINDING     452    452       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00089}.
SQ   SEQUENCE   625 AA;  70172 MW;  D377BF8058E8ECC4 CRC64;
     MNQLTNLSSA EISAQHEQDA KDLTRILPAS KKVYIEGSRP DIQVPMREIS LTDTPTGLGG
     EHNPPIMVYD TSGVYTDPNV QIDLNKGLPS VRQKWIEERN DTDVLSGLTS KFGQERLKDI
     RTADIRFAHI QNPRRAKAGK NVTQMHYAKQ GIITPEMEYI AIRENQRQRE AVDMRQHPGQ
     NFGAKNLKEI TPEFVRQEVA EGRAIIPANI NHPELEPMII GRNFLVKINA NIGNSALGSS
     IDEEVAKMTW ATRWGADTIM DLSTGKNIHE TREWIIRNSP VPIGTVPIYQ ALEKVDGVAE
     NLTWEIFKDT LIEQAEQGVD YFTIHAGVLL RYVPLTANRL TGIVSRGGSI MAQWCLAHHE
     ENFLYTHFDE ICEIMKAYDV SFSLGDGLRP GCIQDANDEA QFSELKTLGE LTHRAWEHDV
     QVMIEGPGHV PMHMIKENMD LQLEVCKEAP FYTLGPLTTD IAPGYDHITS AIGAAMIGWY
     GTAMLCYVTP KEHLGLPNKK DVKDGIITYK IAAHAADLAK GHPGAQVRDN ALSKARFEFR
     WDDQFNLSLD PDTARSMHDE TLPKEAHKSA HFCSMCGPKF CSMKITQNVR DYANNLTNSD
     SEVEEGLKAM KEVYQEQGQK LYHKV
//

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