| Tag | Content |
|---|
| CPLM ID | CPLM-005841 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphomethylpyrimidine synthase |
Protein Synonyms/Alias | Hydroxymethylpyrimidine phosphate synthase; HMP-P synthase; HMP-phosphate synthase; HMPP synthase; Thiamine biosynthesis protein ThiC |
Gene Name | thiC |
Gene Synonyms/Alias | b3994; JW3958 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 31 | GTAFPNSKRIYITGT | acetylation | [1] | | 119 | VRSSDYTKARLADDG | acetylation | [1] | | 507 | EHLGLPNKEDVKQGL | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | 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 | REGION 353 355 Substrate binding (By similarity).
REGION 394 397 Substrate binding (By similarity).
METAL 437 437 Zinc (By similarity).
METAL 501 501 Zinc (By similarity).
METAL 581 581 Iron-sulfur (4Fe-4S-S-AdoMet) (By
METAL 584 584 Iron-sulfur (4Fe-4S-S-AdoMet) (By
METAL 589 589 Iron-sulfur (4Fe-4S-S-AdoMet) (By
BINDING 239 239 Substrate (By similarity).
BINDING 268 268 Substrate (By similarity).
BINDING 297 297 Substrate (By similarity).
BINDING 333 333 Substrate (By similarity).
BINDING 433 433 Substrate (By similarity).
BINDING 460 460 Substrate (By similarity). |
Keyword | 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome; S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 631 AA |
Protein Sequence | MSATKLTRRE QRARAQHFID TLEGTAFPNS KRIYITGTHP GVRVPMREIQ LSPTLIGGSK 60
EQPQYEENEA IPVYDTSGPY GDPQIAINVQ QGLAKLRQPW IDARGDTEEL TVRSSDYTKA 120
RLADDGLDEL RFSGVLTPKR AKAGRRVTQL HYARQGIITP EMEFIAIREN MGRERIRSEV 180
LRHQHPGMSF GAHLPENITA EFVRDEVAAG RAIIPANINH PESEPMIIGR NFLVKVNANI 240
GNSAVTSSIE EEVEKLVWST RWGADTVMDL STGRYIHETR EWILRNSPVP IGTVPIYQAL 300
EKVNGIAEDL TWEAFRDTLL EQAEQGVDYF TIHAGVLLRY VPMTAKRLTG IVSRGGSIMA 360
KWCLSHHQEN FLYQHFREIC EICAAYDVSL SLGDGLRPGS IQDANDEAQF AELHTLGELT 420
KIAWEYDVQV MIEGPGHVPM QMIRRNMTEE LEHCHEAPFY TLGPLTTDIA PGYDHFTSGI 480
GAAMIGWFGC AMLCYVTPKE HLGLPNKEDV KQGLITYKIA AHAADLAKGH PGAQIRDNAM 540
SKARFEFRWE DQFNLALDPF TARAYHDETL PQESGKVAHF CSMCGPKFCS MKISQEVRDY 600
AATQTIEMGM ADMSENFRAR GGEIYLRKEE A 631 |
Gene Ontology | GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. GO:0016829; F:lyase activity; IEA:HAMAP. GO:0008270; F:zinc ion binding; IEA:HAMAP. GO:0009228; P:thiamine biosynthetic process; IEA:HAMAP. GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |