Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q55894 (THIC_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphomethylpyrimidine synthase
EC=4.1.99.17
Alternative name(s):
Hydroxymethylpyrimidine phosphate synthase
Short name=HMP-P synthase
Short name=HMP-phosphate synthase
Short name=HMPP synthase
Thiamine biosynthesis protein ThiC
Gene names
Name:thiC
Ordered Locus Names:slr0118
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis ›

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 By similarity. HAMAP-Rule MF_00089

Catalytic activity

5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO. HAMAP-Rule MF_00089

Cofactor

Binds 1 4Fe-4S cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis. HAMAP-Rule MF_00089

Sequence similarities

Belongs to the ThiC family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Phosphomethylpyrimidine synthase HAMAP-Rule MF_00089
PRO_0000152842

Regions

Region195 – 1973Substrate binding By similarity
Region236 – 2394Substrate binding By similarity

Sites

Metal binding2791Zinc By similarity
Metal binding3431Zinc By similarity
Metal binding4231Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding4261Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding4311Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Binding site801Substrate By similarity
Binding site1091Substrate By similarity
Binding site1391Substrate By similarity
Binding site1751Substrate By similarity
Binding site2751Substrate By similarity
Binding site3021Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q55894 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4819258FC5DBADA8

FASTA45951,137
        10         20         30         40         50         60 
MRTAWVAKRQ GQTNVSQMHY ARKGVITEEM DYVAKRENLP VELIKDEVAR GRMIIPANIN 

        70         80         90        100        110        120 
HTNLEPMAIG IASKCKVNAN IGASPNSSNI DEEVEKLLLS VKYGADTVMD LSTGGGDLDV 

       130        140        150        160        170        180 
IRTAIINASP VPIGTVPIYQ ALESVHGSIE NLTPDDFLHI IEKHAQQGVD YMTIHAGLLI 

       190        200        210        220        230        240 
EYLPLVKSRI TGIVSRGGGI IAKWMLHHHK QNPLYTHFDE IIEIFKKYDV SFSLGDSLRP 

       250        260        270        280        290        300 
GCTHDASDDA QLSELKTLGQ LTRRAWEHDV QVMVEGPGHV PIDQIEFNVK KQMEECSEAP 

       310        320        330        340        350        360 
FYVLGPLVTD IAPGYDHITS AIGAAIAGWH GTAMLCYVTP KEHLGLPNAE DVRNGLIAYK 

       370        380        390        400        410        420 
IAAHAADIAR HRPGARDRDD ELSKARYNFD WNRQFELSLD PERAKEYHDE TLPADIYKTA 

       430        440        450 
EFCSMCGPKF CPMQTKVDAE MLEELEVFLA KDKEMVSQR

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.
[2]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000022 Genomic DNA. Translation: BAA10656.1.
PIRS76712.
RefSeqNP_442586.1. NC_000911.1.
YP_005652647.1. NC_017277.1.
YP_007452462.1. NC_020286.1.

3D structure databases

ProteinModelPortalQ55894.
ModBaseSearch...

Protein-protein interaction databases

IntActQ55894. 1 interaction.
STRING1148.slr0118.

Proteomic databases

PaxDbQ55894.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA10656; BAA10656; BAA10656.
GeneID12254041.
14618144.
952254.
KEGGsyn:slr0118.
syy:SYNGTS_2694.
PATRIC23842900. VBISynSp132158_2988.

Phylogenomic databases

eggNOGCOG0422.
HOGENOMHOG000224483.
KOK03147.
OMAFDWNKQF.
ProtClustDBPRK13352.

Enzyme and pathway databases

UniPathwayUPA00060.

Family and domain databases

HAMAPMF_00089. ThiC.
InterProIPR002817. ThiC.
[Graphical view]
PfamPF01964. ThiC. 1 hit.
[Graphical view]
TIGRFAMsTIGR00190. thiC. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHIC_SYNY3
AccessionPrimary (citable) accession number: Q55894
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents