Q7M818 (THIC_WOLSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	WS1941

Organism

Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes) [Complete proteome] [HAMAP]

Taxonomic identifier

273121 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Wolinella › Wolinella succinogenes

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Protein existence	Inferred 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
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the ThiC family.

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	thiamine biosynthetic process Inferred from electronic annotation. Source: HAMAP thiamine diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW lyase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 449	449	Phosphomethylpyrimidine synthase HAMAP-Rule MF_00089		PRO_0000152850
Regions
	Region	194 – 196	3	Substrate binding By similarity
	Region	235 – 238	4	Substrate binding By similarity
Sites
	Metal binding	278	1	Zinc By similarity
	Metal binding	342	1	Zinc By similarity
	Metal binding	422	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	425	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	430	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Binding site	80	1	Substrate By similarity
	Binding site	109	1	Substrate By similarity
	Binding site	138	1	Substrate By similarity
	Binding site	174	1	Substrate By similarity
	Binding site	274	1	Substrate By similarity
	Binding site	301	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7M818 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: DB137D4EFE4DB6A1	FASTA	449	49,657
	10 20 30 40 50 60 MRQSWIEKRK NDSVRTQLHY ARAGIITEEM QAVANVEGLS EELIRSEVAR GRLVIPANIH 70 80 90 100 110 120 HLSLSPMGIG VAARTKINAN IGSSSLASCI EEEIEKTLVS IKYGADTIMD LSTGGDLDAI 130 140 150 160 170 180 RCAVIEHSSV PIGTVPIYQI LHDVQGDIKN LTIDSMLEVM ERQARQGVSY FTIHCGFLLE 190 200 210 220 230 240 HLPKVAKRKM GIVSRGGSLM ASYMMHYHKQ NPFYEAFDEI LAICREYDVT LSLGDSLRPG 250 260 270 280 290 300 CLADASDEAQ LAELKVLGEL TLRAWEKDVQ VMIEGPGHVP MNQIERNVKL QKELCHEAPF 310 320 330 340 350 360 YVLGPLVTDI AAGYDHIASA IGAAIAAWKG VAMLCYVTPK EHLGLPNAKD VREGILAYKI 370 380 390 400 410 420 AAHAADIARG RIGARDRDDA MSDARYAFDW NRQFELALDP DRAKEYHDES LPQEVFKEAK 430 440 FCSMCGPKFC SYKISQEIVS KHASGESLT

References

[1]

"Complete genome sequence and analysis of Wolinella succinogenes." Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., Meyer F., Lederer H., Schuster S.C. Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571662 Genomic DNA. Translation: CAE10947.1.
RefSeq	NP_908047.1. NC_005090.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	273121.WS1941.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAE10947; CAE10947; WS1941.
GeneID	2554016.
KEGG	wsu:WS1941.
PATRIC	24040822. VBIWolSuc63014_1823.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0422.
HOGENOM	HOG000224483.
KO	K03147.
OMA	FDWNKQF.
ProtClustDB	PRK13352.
Enzyme and pathway databases
UniPathway	UPA00060.
Family and domain databases
HAMAP	MF_00089. ThiC.
InterPro	IPR002817. ThiC. [Graphical view]
Pfam	PF01964. ThiC. 1 hit. [Graphical view]
TIGRFAMs	TIGR00190. thiC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

THIC_WOLSU

Accession

Primary (citable) accession number: Q7M818

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	December 15, 2003
Last modified:	May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program