A5I7P9 (FTHS_CLOBH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Formate--tetrahydrofolate ligase
EC=6.3.4.3

Alternative name(s):
Formyltetrahydrofolate synthetase
Short name=FHS
Short name=FTHFS

Gene names

Name:	fhs
Ordered Locus Names:	CBO3523, CLC_3487

Organism

Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) [Reference proteome] [HAMAP]

Taxonomic identifier

441771 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium botulinum › Clostridium botulinum A

Protein attributes

Sequence length	557 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate. HAMAP-Rule MF_01543
Pathway	One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_01543
Sequence similarities	Belongs to the formate--tetrahydrofolate ligase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	folic acid-containing compound biosynthetic process Inferred from electronic annotation. Source: InterPro tetrahydrofolate interconversion Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP formate-tetrahydrofolate ligase activity 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 – 557	557	Formate--tetrahydrofolate ligase HAMAP-Rule MF_01543		PRO_0000318567
Regions
	Nucleotide binding	66 – 73	8	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5I7P9 [UniParc]. Last modified June 26, 2007. Version 1. Checksum: 5C492C25ED2B538C	FASTA	557	60,743
	10 20 30 40 50 60 MFKSDIEIAQ ESKMKNIKNI AEKIGLTEED IDLYGKYKCK ISLDVLKRNK DKKDGKLILV 70 80 90 100 110 120 TAINPTPAGE GKSTVTVGLG QALWKKNKKA VIALREPSLG PVFGIKGGAA GGGYSQVVPM 130 140 150 160 170 180 EDINLHFTGD MHAITSANNL LAAAIDNHIH QGNILKIDQR RILFKRVMDM NDRALRNVIV 190 200 210 220 230 240 ALGGKINGFP REDGFMITVA SEIMAILCLA EDLMDLKNKM GEILVAYSTE GKPIYCEDLE 250 260 270 280 290 300 VQGAMALLMK DAIKPNLVQT LENTPAIIHG GPFANIAHGC NSILGTKMAL KLGDYVITEA 310 320 330 340 350 360 GFGADLGAEK FFDIKCRKAN LKPNCVVIVA TVRALKYNGG IPKENLKEQN MEALSKGIKN 370 380 390 400 410 420 LGKHIENVNK FGVPAVVAIN KFISDTEEEI EFIKKYCKEL GAEVSIAEVW EKGGNGGLEL 430 440 450 460 470 480 ADKVLDTIEN KESKFNPIYE ETLSIKQKIE TIAEEIYGAE GVDYSKEAEK QISEIEKLDL 490 500 510 520 530 540 DKKPVCMAKT QYSLSDDAKL LGRPCGFRIN VKEVRISNGA GFIVVLTGNV MTMPGLPKKP 550 AANNMNVLSD GNIVGLF

References

[1]

"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes." Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J. Genome Res. 17:1082-1092(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

[2]

"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids." Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S. PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000727 Genomic DNA. Translation: ABS38805.1. AM412317 Genomic DNA. Translation: CAL85084.1.
RefSeq	YP_001256005.1. NC_009495.1. YP_001389246.1. NC_009698.1.
3D structure databases
ProteinModelPortal	A5I7P9.
SMR	A5I7P9. Positions 5-555.
ModBase	Search...
Protein-protein interaction databases
STRING	413999.CBO3523.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABS38805; ABS38805; CLC_3487.
GeneID	5187153. 5400453.
KEGG	cbh:CLC_3487. cbo:CBO3523.
PATRIC	19369205. VBICloBot22612_3501.
Phylogenomic databases
eggNOG	COG2759.
HOGENOM	HOG000040280.
KO	K01938.
OMA	EIMAVLC.
ProtClustDB	PRK13505.
Enzyme and pathway databases
BioCyc	CBOT413999:GJ72-3670-MONOMER. CBOT441771:GIWX-3428-MONOMER.
UniPathway	UPA00193.
Family and domain databases
HAMAP	MF_01543. FTHFS.
InterPro	IPR000559. Formate_THF_ligase. IPR020628. Formate_THF_ligase_CS. [Graphical view]
Pfam	PF01268. FTHFS. 1 hit. [Graphical view]
PROSITE	PS00721. FTHFS_1. 1 hit. PS00722. FTHFS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FTHS_CLOBH

Accession

Primary (citable) accession number: A5I7P9
Secondary accession number(s): A7G8Y1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	June 26, 2007
Last modified:	May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program