Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphomethylpyrimidine synthase

Gene

thiC

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
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)DescriptionActionsGraphical viewLength
Binding sitei80SubstrateUniRule annotation1
Binding sitei109SubstrateUniRule annotation1
Binding sitei139SubstrateUniRule annotation1
Binding sitei175SubstrateUniRule annotation1
Binding sitei275SubstrateUniRule annotation1
Metal bindingi279ZincUniRule annotation1
Binding sitei302SubstrateUniRule annotation1
Metal bindingi343ZincUniRule annotation1
Metal bindingi423Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi426Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi431Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation1

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

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:slr0118
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001528421 – 459Phosphomethylpyrimidine synthaseAdd BLAST459

Proteomic databases

PRIDEiQ55894.

Interactioni

Protein-protein interaction databases

IntActiQ55894. 1 interactor.

Structurei

3D structure databases

ProteinModelPortaliQ55894.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni195 – 197Substrate bindingUniRule annotation3
Regioni236 – 239Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the ThiC family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000224483.
InParanoidiQ55894.
KOiK03147.
OMAiHIIEKHC.
PhylomeDBiQ55894.

Family and domain databases

HAMAPiMF_00089. ThiC. 1 hit.
InterProiIPR002817. ThiC.
[Graphical view]
PfamiPF01964. ThiC_Rad_SAM. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00190. thiC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q55894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTAWVAKRQ GQTNVSQMHY ARKGVITEEM DYVAKRENLP VELIKDEVAR
60 70 80 90 100
GRMIIPANIN HTNLEPMAIG IASKCKVNAN IGASPNSSNI DEEVEKLLLS
110 120 130 140 150
VKYGADTVMD LSTGGGDLDV IRTAIINASP VPIGTVPIYQ ALESVHGSIE
160 170 180 190 200
NLTPDDFLHI IEKHAQQGVD YMTIHAGLLI EYLPLVKSRI TGIVSRGGGI
210 220 230 240 250
IAKWMLHHHK QNPLYTHFDE IIEIFKKYDV SFSLGDSLRP GCTHDASDDA
260 270 280 290 300
QLSELKTLGQ LTRRAWEHDV QVMVEGPGHV PIDQIEFNVK KQMEECSEAP
310 320 330 340 350
FYVLGPLVTD IAPGYDHITS AIGAAIAGWH GTAMLCYVTP KEHLGLPNAE
360 370 380 390 400
DVRNGLIAYK IAAHAADIAR HRPGARDRDD ELSKARYNFD WNRQFELSLD
410 420 430 440 450
PERAKEYHDE TLPADIYKTA EFCSMCGPKF CPMQTKVDAE MLEELEVFLA

KDKEMVSQR
Length:459
Mass (Da):51,137
Last modified:November 1, 1996 - v1
Checksum:i4819258FC5DBADA8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10656.1.
PIRiS76712.

Genome annotation databases

EnsemblBacteriaiBAA10656; BAA10656; BAA10656.
KEGGisyn:slr0118.
PATRICi23842900. VBISynSp132158_2988.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10656.1.
PIRiS76712.

3D structure databases

ProteinModelPortaliQ55894.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ55894. 1 interactor.

Proteomic databases

PRIDEiQ55894.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA10656; BAA10656; BAA10656.
KEGGisyn:slr0118.
PATRICi23842900. VBISynSp132158_2988.

Phylogenomic databases

HOGENOMiHOG000224483.
InParanoidiQ55894.
KOiK03147.
OMAiHIIEKHC.
PhylomeDBiQ55894.

Enzyme and pathway databases

UniPathwayiUPA00060.

Family and domain databases

HAMAPiMF_00089. ThiC. 1 hit.
InterProiIPR002817. ThiC.
[Graphical view]
PfamiPF01964. ThiC_Rad_SAM. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00190. thiC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTHIC_SYNY3
AccessioniPrimary (citable) accession number: Q55894
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 101 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
  3. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.