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Protein

Phosphomethylpyrimidine synthase

Gene

thiC

Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
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 sitei237 – 2371SubstrateUniRule annotation
Binding sitei266 – 2661SubstrateUniRule annotation
Binding sitei295 – 2951SubstrateUniRule annotation
Binding sitei331 – 3311SubstrateUniRule annotation
Binding sitei431 – 4311SubstrateUniRule annotation
Metal bindingi435 – 4351ZincUniRule annotation
Binding sitei458 – 4581SubstrateUniRule annotation
Metal bindingi499 – 4991ZincUniRule annotation
Metal bindingi579 – 5791Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi582 – 5821Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi587 – 5871Iron-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

BioCyciCVIO243365:GHUD-235-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:CV_0235
OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Taxonomic identifieri243365 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
Proteomesi
  • UP000001424 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 632632Phosphomethylpyrimidine synthasePRO_0000152795Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi243365.CV_0235.

Structurei

3D structure databases

ProteinModelPortaliQ7P1H8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni351 – 3533Substrate bindingUniRule annotation
Regioni392 – 3954Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the ThiC family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CBF. Bacteria.
COG0422. LUCA.
HOGENOMiHOG000224484.
KOiK03147.
OMAiTWELFRD.
OrthoDBiPOG091H02FB.

Family and domain databases

HAMAPiMF_00089. ThiC. 1 hit.
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.

Q7P1H8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAPVNKQMV VDAAAIQPLP NSRKIYVEGS RPDIQVPMRE IRQADTPTQF
60 70 80 90 100
GGEKNPPIFV YDTSGPYSDP AARIDIQSGL APLRAAWIAQ RGDCEQLPGL
110 120 130 140 150
SSEYGRAREA DPKLAELRFN LQRKPRRAKA GRNVTQMHYA RRGIVTPEME
160 170 180 190 200
FVAIRENLNR RAYVESLQAA GNRRLLDLMT RQHQGQSFGA HLPEEITPEF
210 220 230 240 250
VREEIAAGRA IIPANINHPE SEPMIIGRNF LVKINGNIGN SAVTSSISEE
260 270 280 290 300
VDKMTWGIRW GADTIMDLST GKNIHETREW ILRNSPVPIG TVPIYQALEK
310 320 330 340 350
VNGKAEDLSW EIFRDTLIEQ AEQGVDYFTI HAGVRLAYVP MTANRMTGIV
360 370 380 390 400
SRGGSIMAKW CLAHHRENFL YTHFEDICEI MKAYDVAFSL GDGLRPGSAW
410 420 430 440 450
DANDEAQLSE LKTLGELTEI AWKHDVQVMI EGPGHVPMQL IKENMDKELE
460 470 480 490 500
WCREAPFYTL GPLTTDIAPG YDHITSAIGA AQIGWYGTAM LCYVTQKEHL
510 520 530 540 550
GLPNKHDVKE GIITYKLAAH AADLAKGHPG AQIRDNALSK ARFEFRWEDQ
560 570 580 590 600
FNLGLDPDKA RDFHDETLPK DSAKVAHFCS MCGPHFCSMK ITQDVREYAA
610 620 630
SQGVGEQDAL RLGMREKAIE FVKGGGKLYD KV
Length:632
Mass (Da):70,644
Last modified:December 15, 2003 - v1
Checksum:iFB7308052CE65441
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016825 Genomic DNA. Translation: AAQ57914.1.
RefSeqiWP_011133790.1. NC_005085.1.

Genome annotation databases

EnsemblBacteriaiAAQ57914; AAQ57914; CV_0235.
GeneIDi24946048.
KEGGicvi:CV_0235.
PATRICi21435232. VBIChrVio67196_0227.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016825 Genomic DNA. Translation: AAQ57914.1.
RefSeqiWP_011133790.1. NC_005085.1.

3D structure databases

ProteinModelPortaliQ7P1H8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243365.CV_0235.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAQ57914; AAQ57914; CV_0235.
GeneIDi24946048.
KEGGicvi:CV_0235.
PATRICi21435232. VBIChrVio67196_0227.

Phylogenomic databases

eggNOGiENOG4105CBF. Bacteria.
COG0422. LUCA.
HOGENOMiHOG000224484.
KOiK03147.
OMAiTWELFRD.
OrthoDBiPOG091H02FB.

Enzyme and pathway databases

UniPathwayiUPA00060.
BioCyciCVIO243365:GHUD-235-MONOMER.

Family and domain databases

HAMAPiMF_00089. ThiC. 1 hit.
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...

Entry informationi

Entry nameiTHIC_CHRVO
AccessioniPrimary (citable) accession number: Q7P1H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: December 15, 2003
Last modified: September 7, 2016
This is version 82 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, Reference 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.