Q8FVP6 (FOLD_BRUSU) 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:	BRA0781, BS1330_II0774

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella suis

Protein attributes

Sequence length	299 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
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 – 299	299	Bifunctional protein FolD HAMAP-Rule MF_01576		PRO_0000268296

Sequences

	Sequence		Length	Mass (Da)
	Q8FVP6 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 7446B7B964FB967A	FASTA	299	31,231
	10 20 30 40 50 60 MAQLIDGKKL AEDVVSTVKT ETEKLVAATG VVPGIAVVIV GEDPASQVYV ASKSRKAKEC 70 80 90 100 110 120 GFHSVQHDLP ETASEQELLN LIEGLNNDPA IHGILVQLPL PGHIDSGRVI QTIAPEKDVD 130 140 150 160 170 180 GFHFINVGKL GTGEVETAFV PCTPAGAMIM IERVHGRDLS GLNAVVIGRS NIVGKPMFNL 190 200 210 220 230 240 LLAANATVTV AHSRTKDLPA IARNADILVA AVGRPQMVKG DWVKPGATVI DVGINRIPAP 250 260 270 280 290 ERGEGKTRLV GDVDFAEAEK VAGAITPVPG GVGPMTIAML MANTLTAACR SAGMKKPVF

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014292 Genomic DNA. Translation: AAN33961.1. CP002998 Genomic DNA. Translation: AEM20237.1.
RefSeq	NP_699956.1. NC_004311.2. YP_005614463.1. NC_017250.1.
3D structure databases
HSSP	HSSP built from PDB template 1A4I based on UniProtKB P11586.
ProteinModelPortal	Q8FVP6.
SMR	Q8FVP6. Positions 2-292.
ModBase	Search...
Protein-protein interaction databases
STRING	204722.BRA0781.
Proteomic databases
PRIDE	Q8FVP6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN33961; AAN33961; BRA0781. AEM20237; AEM20237; BS1330_II0774.
GeneID	1165223. 12139002.
KEGG	bms:BRA0781. bsi:BS1330_II0774.
PATRIC	17794369. VBIBruSui107850_2995.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0190.
HOGENOM	HOG000218242.
KO	K01491.
OMA	CKHEIDA.
ProtClustDB	PRK14188.
Enzyme and pathway databases
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. 1 hit. PS00767. THF_DHG_CYH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLD_BRUSU

Accession

Primary (citable) accession number: Q8FVP6
Secondary accession number(s): G0KDE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program