Reviewed, UniProtKB/Swiss-Prot Q7W4Z7 (FOLD2_BORPA)

Names and origin

Protein names

Recommended name:
    Bifunctional protein folD 2
Including the following 2 domains:
    1- Recommended name:
            Methylenetetrahydrofolate dehydrogenase
              EC=1.5.1.5
    2- Recommended name:
            Methenyltetrahydrofolate cyclohydrolase
              EC=3.5.4.9

Gene names

Name:	folD2
Ordered Locus Names:	BPP3509

Organism

Bordetella parapertussis [Complete proteome] [HAMAP]

Taxonomic identifier

519 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	5,10-methylenetetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH. 5,10-methenyltetrahydrofolate + H(2)O = 10-formyltetrahydrofolate.
Pathway	One-carbon metabolism; tetrahydrofolate pathway.
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 and derivative 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 one-carbon compound metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro methenyltetrahydrofolate cyclohydrolase activity Inferred from electronic annotation. Source: HAMAP methylenetetrahydrofolate dehydrogenase (NADP+) 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 – 283	283	Bifunctional protein folD 2		PRO_0000268286

Sequences

	Sequence		Length	Mass (Da)
	Q7W4Z7-1 [UniParc]. Last modified December 12, 2006. Version 2. Checksum: 2A1E630EE1F64C7F	FASTA	283	29,520
	10 20 30 40 50 60 MKDKVIDGSR ASARIREQLK ERVACLRARN IRPGLAVLLV GEDPASQVYV RNKVAACEQV 70 80 90 100 110 120 GIHSVTERYP SAWTENQLLD RIASLNGDPA INGILVQLPL PPHMSAHRVI EAISPLKDVD 130 140 150 160 170 180 GFHISNAGLL MTGKPQFQPC TPYGVMKLLE SEGVSLRGAE AVIVGASNIV GKPMAMLLLA 190 200 210 220 230 240 AGATVTICNS KTRDLAGQAR RADVLIVAAG RAGIVDGSMI KPGAVVIDVG INRGPDGRLC 250 260 270 280 GDVDYGSAAK VAGAITPVPG GVGPMTIAML LANTVEAAER SAI

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640433 Genomic DNA. Translation: CAE38793.1. Different initiation.
RefSeq	NP_885669.1.
3D structure databases
HSSP	HSSP built from PDB template 1A4I based on UniProtKB P11586.
ModBase	Search...
Genome annotation databases
GeneID	1664611.
GenomeReviews	Gene locus BPP3509 in contig BX470249_GR.
KEGG	bpa:BPP3509.
NMPDR	fig|257311.1.peg.3303.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7W4Z7.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP3509-MON.
Family and domain databases
HAMAP	MF_01576. [Tree]
InterPro	IPR000672. THF_DHase/CycOHase. [Graphical view]
Pfam	PF00763. THF_DHG_CYH. 1 hit. PF02882. THF_DHG_CYH_C. 1 hit. [Graphical view]
PRINTS	PR00085. THFDHDRGNASE.
ProDom	PD002300. THFDhg/Cyc_hydro. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00766. THF_DHG_CYH_1. 1 hit. PS00767. THF_DHG_CYH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLD2_BORPA

Accession

Primary (citable) accession number: Q7W4Z7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	December 12, 2006
Last modified:	November 25, 2008
This is version 31 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)