Q0S375 (FOLD2_RHOSR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional protein FolD 2

Including the following 2 domains:

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

Gene names

Name:	folD2
Ordered Locus Names:	RHA1_ro06234

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	286 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 MF_01576
Catalytic activity	5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH. HAMAP MF_01576 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. HAMAP MF_01576
Pathway	One-carbon metabolism; tetrahydrofolate interconversion. HAMAP MF_01576
Subunit structure	Homodimer By similarity. HAMAP MF_01576
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 one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	methenyltetrahydrofolate cyclohydrolase activity Inferred from electronic annotation. Source: EC methylenetetrahydrofolate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC 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 – 286	286	Bifunctional protein FolD 2 HAMAP MF_01576		PRO_0000268471

Sequences

	Sequence		Length	Mass (Da)
	Q0S375 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: BD9181AD66BCBA4F	FASTA	286	30,097
	10 20 30 40 50 60 MTATILDGKA TRDEIFEDLK VRVSALKDRG ITPGLGTVLV GDDPGSAAYV RGKHNDCAKV 70 80 90 100 110 120 GITSIRRDLP GDITQEKLDA TIDELNANPD CTGYIVQLPL PKQLDENAAL ERIDPDKDAD 130 140 150 160 170 180 GLHPVNLGRL VLGKKAPLPC TPRGILHLLR RYEVPIEGAH VVVVGRGVTV GRPIGLLFTR 190 200 210 220 230 240 RSENATVTLC HTRTRDLGAE VRRADIVIAA AGVPGLITAD MVKPGAAVLD VGVSRTADGL 250 260 270 280 RGDVAADVAE VAGFLSPNPG GVGPLTRAFL LTNVVERAER VAASLG

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]. Strain: RHA1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000431 Genomic DNA. Translation: ABG98011.1.
RefSeq	YP_706169.1. NC_008268.1.
3D structure databases
ProteinModelPortal	Q0S375.
SMR	Q0S375. Positions 3-280.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0S375.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4223785.
GenomeReviews	Gene locus RHA1_ro06234 in contig CP000431_GR.
KEGG	rha:RHA1_ro06234.
PATRIC	23211413. VBIRhoJos26306_6282.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0190.
HOGENOM	HBG328751.
OMA	LLMKENA.
ProtClustDB	PRK14193.
Enzyme and pathway databases
BioCyc	RSP101510:RHA1_RO06234-MONOMER.
Family and domain databases
HAMAP	MF_01576. THF_DHG_CYH. [Tree]
InterPro	IPR016040. NAD(P)-bd_dom. IPR000672. THF_DH/CycHdrlase. IPR020630. THF_DH/CycHdrlase_cat_dom. IPR020631. THF_DH/CycHdrlase_NAD-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K01491.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLD2_RHOSR

Accession

Primary (citable) accession number: Q0S375

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program