(data stored in ACNUC30567 zone)

HOGENOM: ACAM1_1_PE2909

ID   ACAM1_1_PE2909                       STANDARD;      PRT;   458 AA.
AC   ACAM1_1_PE2909; B0CCG9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Phosphomethylpyrimidine synthase; EC=4.-.- -;AltName:
DE   Full=Hydroxymethylpyrimidine phosphate synthase; Short=HMP-P synthase;
DE   Short=HMP-phosphate synthase; Short=HMPP synthase;AltName: Full=Thiamine
DE   biosynthesis protein thiC; (ACAM1_1.PE2909).
GN   Name=thiC; OrderedLocusNames=AM1_3002;
OS   ACARYOCHLORIS MARINA MBIC11017.
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACAM1_1.PE2909.
CC       Acaryochloris marina MBIC11017, complete genome.
CC   -!- ANNOTATIONS ORIGIN:THIC_ACAM1
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.
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   -!- MISCELLANEOUS: The reaction is still not fully elucidated. Not all
CC       reaction products are known. The shown reaction is thus not
CC       balanced.
CC   -!- SIMILARITY: Belongs to the thiC family.
CC   -!- GENE_FAMILY: HOG000224483 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0CCG9; -.
DR   EMBL; CP000828; ABW27998.1; -; Genomic_DNA.
DR   RefSeq; YP_001517314.1; NC_009925.1.
DR   STRING; B0CCG9; -.
DR   GeneID; 5681810; -.
DR   GenomeReviews; CP000828_GR; AM1_3002.
DR   KEGG; amr:AM1_3002; -.
DR   OMA; DFLHIIE; -.
DR   ProtClustDB; PRK13352; -.
DR   BioCyc; AMAR329726:AM1_3002-MON; -.
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   HAMAP; MF_00089; ThiC; 1; -.
DR   InterPro; IPR002817; ThiC.
DR   Pfam; PF01964; ThiC; 1.
DR   TIGRFAMs; TIGR00190; ThiC; 1.
DR   HOGENOMDNA; ACAM1_1.PE2909; -.
KW   thiamine biosynthesis protein ThiC;
KW   4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding;
KW   S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc.
SQ   SEQUENCE   458 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRHQWVANRR GQSNVSQMHY ARQGQITEEM DYVAKRENLP ADLIREEVAR GRMIIPANVN
     HVNLEPMAIG IASKCKVNAN IGASPNSSNI EEELDKLRLA VKYGADTVMD LSTGGGNLDE
     IRTAIINESS VPIGTVPIYQ ALESVHGNIE NLTADDFLHI IDKHAQQGVD YQTIHAGILI
     EHLPLVRDRI TGIVSRGGGI LARWMLHHHK QNPLYTRFND VIEIFKKHDV SFSLGDSLRP
     GCTHDASDDA QLAELKTLGQ LTRRAWEHDV QVMVEGPGHV PMDQIEFNVR KQMEECSEAP
     FYVLGPLVTD IAPGYDHITS AIGAAMAGWY GTAMLCYVTP KEHLGLPDAE DVRNGLIAYK
     IAAHAADIAR HRPGARDRDD QLSEARYNFD WNRQFELSLD PERAREYHDE TLPADIYKTA
     EFCSMCGPKF CPMQTKVDAD ALTELEKFLA KDQVGSAR
//

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