※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphomethylpyrimidine synthase
Protein Synonyms/Alias
 HMP-P synthase;  HMP-phosphate synthase;  HMPP synthase
Gene Name
 thiC
Gene Synonyms/Alias
 thiA; OrderedLocusNames=BSU08790
Created Date
 3-June-2014
Organism
 Bacillus subtilis (strain 168)
NCBI Taxa ID
 224308
Phosphorylation
Position
Peptide
Code
Type
References
586 KEFVDTGSNLYQMQN S HTP [1]
589 VDTGSNLYQMQNNSV Y HTP [1]
565 YAKKNDLSEAEAINK S HTP [1]
556 MRISQDIRDYAKKND R HTP [2]
Reference
 [1]Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis.
 Soufi B,Kumar C,Gnad F,Mann M,Mijakovic I,Macek B
 J. Proteome Res. 2010, Jul, 2;9(7):3638-46. [PMID:20509597]
 [2]Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
 Elsholz AK,Turgay K,Michalik S,Hessling B,Gronau K,Oertel D,Mäder U,Bernhardt J,Becher D,Hecker M,Gerth U
 Proc. Natl. Acad. Sci. U.S.A. 2012, May, 8;109(19):7451-6. [PMID:22517742]
Functional Description From UniProt
 FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction (Probable)
Sequence Annotation From UniProt
 
Key Word From UniProt
 4Fe-4S; Completeproteome; Iron; Iron-sulfur; Lyase; Metal-binding; Referenceproteome; S-adenosyl-L-methionine; Thiaminebiosynthesis; Zinc
Protein Sequence
 MQNNSVQQAN ISIMSSFSGS KKVYVEGSSS DIQVPMREIA LSPTTGSFGE EENAPVRVYD 60
 TSGPYTDPEV TINIQEGLKP LRQKWITERG DVEEYEGRAI KPEDNGYKKA KPNVSYPGLK 120
 RKPLRAKAGQ NVTQMHYAKK GIITPEMEFI AIREHVSPEF VRDEVASGRA IIPSNINHPE 180
 SEPMIIGRNF HVKINANIGN SAVTSSIEEE VEKMTWAIRW GADTMMDLST GKDIHTTREW 240
 IIRNCPVPVG TVPIYQALEK VNGVAEDLTW EIYRDTLIEQ AEQGVDYFTI HAGVLLRYVP 300
 LTAKRTTGIV SRGGAIMAQW CLAHHQESFL YTHFEEICEI MKMYDIAFSL GDGLRPGSIA 360
 DANDEAQFAE LETLGELTQI AWKHDVQVMI EGPGHVPMHK IKENVDKQMD ICKEAPFYTL 420
 GPLTTDIAPG YDHITSAIGA AMIGWYGTAM LCYVTPKEHL GLPNRDDVRE GVITYKIAAH 480
 AADLAKGHPG AQIRDDALSK ARFEFRWRDQ FNLSLDPERA LEYHDETLPA EGAKTAHFCS 540
 MCGPKFCSMR ISQDIRDYAK KNDLSEAEAI NKGLKEKAKE FVDTGSNLYQ 590
  GO:0051539   F:4 iron, 4 sulfur cluster binding IEA:UniProtKB-KW
  GO:0016829   F:lyase activity IEA:UniProtKB-HAMAP
  GO:0008270   F:zinc ion binding IEA:UniProtKB-HAMAP
  GO:0009228   P:thiamine biosynthetic process IEA:UniProtKB-HAMAP
  GO:0009229   P:thiamine diphosphate biosynthetic process IEA:UniProtKB-UniPathway
  IPR002817   ThiC.
  IPR025747   ThiC-associated_dom.
  PF01964   ThiC.
  PF13667   ThiC-associated.