Q83EK7 (FOLD_COXBU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional protein FolD

Including the following 2 domains:

1. Methylenetetrahydrofolate dehydrogenase
   EC=1.5.1.5
2. Methenyltetrahydrofolate cyclohydrolase
   EC=3.5.4.9

Gene names

Name:	folD
Ordered Locus Names:	CBU_0312

Organism

Coxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]

Taxonomic identifier

227377 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella › Coxiella burnetii

Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate By similarity. HAMAP-Rule MF_01576
Catalytic activity	5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH. HAMAP-Rule MF_01576 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. HAMAP-Rule MF_01576
Pathway	One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_01576
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis Methionine biosynthesis One-carbon metabolism Purine biosynthesis
Ligand	NADP
Molecular function	Hydrolase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	folic acid-containing compound biosynthetic process Inferred from electronic annotation. Source: InterPro histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate interconversion Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	methenyltetrahydrofolate cyclohydrolase activity Inferred from electronic annotation. Source: HAMAP methylenetetrahydrofolate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: HAMAP nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 283	283	Bifunctional protein FolD HAMAP-Rule MF_01576		PRO_0000268327

Sequences

	Sequence		Length	Mass (Da)
	Q83EK7 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: AA81B2B09EE7A2B2	FASTA	283	30,820
	10 20 30 40 50 60 MIARILDGRT CAEKVKARVK ENIRLLQEKG LPSPGLAVIL VGNDPASATY VAHKERACQA 70 80 90 100 110 120 VGIRSTVYRM PNTITESELA SKIDECNRDS NTHGILLQLP LPAHIDPANL LERIRPDKDV 130 140 150 160 170 180 DGFHPYNLGR LVQRRPALRP CTPYGVMTLL TETHENLEGK HAVIVGASNI VGRPMALELL 190 200 210 220 230 240 LAKCTVTVCH RFTRDLAEHV KSAELLIVAI GKPGIIQSEW IKPGAIVIDV GFSRLSPNKI 250 260 270 280 AGDIDFETAK ERASWITPVP GGVGPMTVAT LLENTLQAAQ TFL

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RSA 493 / Nine Mile phase I.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016828 Genomic DNA. Translation: AAO89869.1.
RefSeq	NP_819355.1. NC_002971.3.
3D structure databases
HSSP	HSSP built from PDB template 1A4I based on UniProtKB P11586.
ProteinModelPortal	Q83EK7.
SMR	Q83EK7. Positions 3-278.
ModBase	Search...
Protein-protein interaction databases
STRING	227377.CBU_0312.
Proteomic databases
PRIDE	Q83EK7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO89869; AAO89869; CBU_0312.
GeneID	1208194.
KEGG	cbu:CBU_0312.
PATRIC	17929313. VBICoxBur82552_0304.
Phylogenomic databases
eggNOG	COG0190.
HOGENOM	HOG000218242.
KO	K01491.
OMA	EDTSIHG.
ProtClustDB	PRK10792.
Enzyme and pathway databases
BioCyc	CBUR227377:GJ7S-318-MONOMER.
UniPathway	UPA00193.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_01576. THF_DHG_CYH.
InterPro	IPR016040. NAD(P)-bd_dom. IPR000672. THF_DH/CycHdrlase. IPR020630. THF_DH/CycHdrlase_cat_dom. IPR020867. THF_DH/CycHdrlase_CS. IPR020631. THF_DH/CycHdrlase_NAD-bd_dom. [Graphical view]
Pfam	PF00763. THF_DHG_CYH. 1 hit. PF02882. THF_DHG_CYH_C. 1 hit. [Graphical view]
PRINTS	PR00085. THFDHDRGNASE.
PROSITE	PS00766. THF_DHG_CYH_1. False negative. PS00767. THF_DHG_CYH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLD_COXBU

Accession

Primary (citable) accession number: Q83EK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program