Reviewed, UniProtKB/Swiss-Prot Q7VZC8 (FOLD1_BORPE)

Names and origin

Protein names

Recommended name:
    Bifunctional protein folD 1
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:	folD1
Ordered Locus Names:	BP0990

Organism

Bordetella pertussis [Complete proteome] [HAMAP]

Taxonomic identifier

520 [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 1		PRO_0000268287

Sequences

	Sequence		Length	Mass (Da)
	Q7VZC8-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 222B55348C370356	FASTA	283	29,489
	10 20 30 40 50 60 MTARIIDGAA LSQRIREEVA QRVQALTAKG VRPGLAVVLV GDDPASQVYV RNKVAACEKA 70 80 90 100 110 120 GLHSVKEQYP ADLTEAQLLE RIDALNRDPS IHGILVQLPL PRHMDAHKVI EAIAAEKDVD 130 140 150 160 170 180 GFHISNAGLL MTGQPLFRPC TPYGVMKMLE SEGVALRGAE AVIVGASNIV GKPMAMLLLQ 190 200 210 220 230 240 AGATITICNS KTRDLGAQTR RADVLVVATG KPGMIDGSMI KPGAVVIDVG INRGADGKLC 250 260 270 280 GDVDMASARE VAGAISPVPG GVGPMTIAML LVNTVEAAER AAA

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: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640413 Genomic DNA. Translation: CAE41291.1.
RefSeq	NP_879784.1.
3D structure databases
HSSP	HSSP built from PDB template 1A4I based on UniProtKB P11586.
ModBase	Search...
Genome annotation databases
GeneID	2664077.
GenomeReviews	Gene locus BP0990 in contig BX470248_GR.
KEGG	bpe:BP0990.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7VZC8.
Enzyme and pathway databases
BioCyc	BPER257313:BP0990-MON.
Family and domain databases
HAMAP	MF_01576. [Tree]
InterPro	IPR016040. NAD(P)-bd. IPR000672. THF_DHase/CycOHase. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
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

FOLD1_BORPE

Accession

Primary (citable) accession number: Q7VZC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	October 1, 2003
Last modified:	November 25, 2008
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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