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Protein

Phosphomethylpyrimidine synthase

Gene

thiC

Organism
Salmonella schwarzengrund (strain CVM19633)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphomethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Pathwayi: thiamine diphosphate biosynthesis

This protein is involved in the pathway thiamine diphosphate biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei239 – 2391SubstrateUniRule annotation
Binding sitei268 – 2681SubstrateUniRule annotation
Binding sitei297 – 2971SubstrateUniRule annotation
Binding sitei333 – 3331SubstrateUniRule annotation
Binding sitei433 – 4331SubstrateUniRule annotation
Metal bindingi437 – 4371ZincUniRule annotation
Binding sitei460 – 4601SubstrateUniRule annotation
Metal bindingi501 – 5011ZincUniRule annotation
Metal bindingi581 – 5811Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi584 – 5841Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi589 – 5891Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BioCyciSENT439843:GHHR-704-MONOMER.
UniPathwayiUPA00060.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomethylpyrimidine synthaseUniRule annotation (EC:4.1.99.17UniRule annotation)
Alternative name(s):
Hydroxymethylpyrimidine phosphate synthaseUniRule annotation
Short name:
HMP-P synthaseUniRule annotation
Short name:
HMP-phosphate synthaseUniRule annotation
Short name:
HMPP synthaseUniRule annotation
Thiamine biosynthesis protein ThiCUniRule annotation
Gene namesi
Name:thiCUniRule annotation
Ordered Locus Names:SeSA_A4374
OrganismiSalmonella schwarzengrund (strain CVM19633)
Taxonomic identifieri439843 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001865 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 631631Phosphomethylpyrimidine synthasePRO_1000093234Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB4TQK4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni353 – 3553Substrate bindingUniRule annotation
Regioni394 – 3974Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the ThiC family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000224484.
KOiK03147.
OMAiTWELFRD.
OrthoDBiEOG6NWBM5.

Family and domain databases

HAMAPiMF_00089. ThiC.
InterProiIPR002817. ThiC.
IPR025747. ThiC-associated_dom.
[Graphical view]
PfamiPF13667. ThiC-associated. 1 hit.
PF01964. ThiC_Rad_SAM. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00190. thiC. 1 hit.

Sequencei

Sequence statusi: Complete.

B4TQK4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTTTLTRRE QRAKAQHFID TLEGTAFPNS KRIYVTGSQH DIRVPMREIQ
60 70 80 90 100
LSPTLIGGSK DNPQFEENEA VPVYDTSGPY GDPEVAINVQ QGLAKLRQPW
110 120 130 140 150
IDARNDSEEL DDRSSAYTRE RLADDGLDDL RFTGLLTPKR AKAGKRVTQL
160 170 180 190 200
HYARNGIVTP EMEFIAIREN MGRERIRSEV LRHQHPGMSF GARLPENITP
210 220 230 240 250
EFVRDEVAAG RAIIPANINH PESEPMIIGR NFLVKVNANI GNSAVTSSIE
260 270 280 290 300
EEVEKLVWAT RWGADTVMDL STGRYIHETR EWILRNSPVP IGTVPIYQAL
310 320 330 340 350
EKVNGIAEDL TWEAFRDTLL EQAEQGVDYF TIHAGVLLRY VPMTAKRLTG
360 370 380 390 400
IVSRGGSIMA KWCLSHHKEN FLFEHFREIC EICAAYDVSL SLGDGLRPGS
410 420 430 440 450
IQDANDEAQF SELHTLGELT KIAWEYDVQV MIEGPGHVPM HMIQRNMTEE
460 470 480 490 500
LEHCHEAPFY TLGPLTTDIA PGYDHFTSGI GAAMIGWFGC AMLCYVTPKE
510 520 530 540 550
HLGLPNKEDV KQGLITYKIA AHAADLAKGH PGAQIRDNAM SKARFEFRWE
560 570 580 590 600
DQFNLALDPF TARAWHDETL PQESGKVAHF CSMCGPKFCS MKISQEVRDY
610 620 630
AAAQTIEVGM ADMSENFRAK GGEIYLKREE V
Length:631
Mass (Da):70,874
Last modified:September 23, 2008 - v1
Checksum:i682A964C7A468E8D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001127 Genomic DNA. Translation: ACF89304.1.
RefSeqiWP_000108416.1. NC_011094.1.

Genome annotation databases

EnsemblBacteriaiACF89304; ACF89304; SeSA_A4374.
KEGGisew:SeSA_A4374.
PATRICi32377305. VBISalEnt87589_4336.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001127 Genomic DNA. Translation: ACF89304.1.
RefSeqiWP_000108416.1. NC_011094.1.

3D structure databases

ProteinModelPortaliB4TQK4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACF89304; ACF89304; SeSA_A4374.
KEGGisew:SeSA_A4374.
PATRICi32377305. VBISalEnt87589_4336.

Phylogenomic databases

HOGENOMiHOG000224484.
KOiK03147.
OMAiTWELFRD.
OrthoDBiEOG6NWBM5.

Enzyme and pathway databases

UniPathwayiUPA00060.
BioCyciSENT439843:GHHR-704-MONOMER.

Family and domain databases

HAMAPiMF_00089. ThiC.
InterProiIPR002817. ThiC.
IPR025747. ThiC-associated_dom.
[Graphical view]
PfamiPF13667. ThiC-associated. 1 hit.
PF01964. ThiC_Rad_SAM. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00190. thiC. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
    Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
    J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CVM19633.

Entry informationi

Entry nameiTHIC_SALSV
AccessioniPrimary (citable) accession number: B4TQK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: February 17, 2016
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.