Reviewed, UniProtKB/Swiss-Prot Q0SFQ8 (FOLD1_RHOSR)

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:	RHA1_ro01817

Organism

Rhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP]

Taxonomic identifier

101510 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	297 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 – 297	297	Bifunctional protein folD 1		PRO_0000268470

Sequences

	Sequence		Length	Mass (Da)
	Q0SFQ8-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: D5613791E94D4C1A	FASTA	297	30,064
	10 20 30 40 50 60 MTRSLGGAEL ATSIRNDASV AAAALNDLGT RPKLAVVQAT DDESTAWYVR SIASAAKRTG 70 80 90 100 110 120 ILCDIVDLGA AASTEQIRST LVELGHDPDV HGIILQTPLP DGTDLDALRE AINPAKDVDG 130 140 150 160 170 180 ANPVSLGRLV ARLPAFAPAT AQAVIALLDH HGISPHARTA TVVGRSTVVG SPVAHLLVQR 190 200 210 220 230 240 NATVTVCHRH TTDLAAGTRD ADILVVAVGI PGLITADHVA DGAVVIDVGT TATADGQLLG 250 260 270 280 290 DVDAAAVDGR AGALTPVPGG VGPVTTALLL NHTVDAAGTQ YAQTRSESVL AGFRSSV

References

[1]

"The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse." McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H. , Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W., Eltis L.D. Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006) [PubMed: 17030794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000431 Genomic DNA. Translation: ABG93628.1.
RefSeq	YP_701786.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4218747.
GenomeReviews	Gene locus RHA1_ro01817 in contig CP000431_GR.
KEGG	rha:RHA1_ro01817.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0SFQ8.
Enzyme and pathway databases
BioCyc	RSP101510:RHA1_RO01817-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. False negative. PS00767. THF_DHG_CYH_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLD1_RHOSR

Accession

Primary (citable) accession number: Q0SFQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	September 5, 2006
Last modified:	November 25, 2008
This is version 19 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)