Reviewed, UniProtKB/Swiss-Prot Q6F8N7 (FOLD2_ACIAD)

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:	ACIAD2847

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	282 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 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 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 – 282	282	Bifunctional protein folD 2 HAMAP MF_01576		PRO_0000268253

Sequences

	Sequence		Length	Mass (Da)
	Q6F8N7-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: A214E40FA8CA6413	FASTA	282	29,540
	10 20 30 40 50 60 MALVLDGRAL AKKIEADLLV RVEALKAKSG RTPILATILV GDDGASATYV RMKGNACRRV 70 80 90 100 110 120 GMDSLKIELS QETTTEQLLA EIEKLNANPD VHGILLQHPV PAQIDERACF DAISLAKDVD 130 140 150 160 170 180 GVTCLGYGRM AMGEAAYGSA TPAGIMTILK ENNIEIAGKH AVVVGRSAIL GKPMAAMLLE 190 200 210 220 230 240 ANATVTICHS RTQNLAEFVK QADIIVGAVG KAELIQKDWI KPGAVVVDAG FHPRDGGGVG 250 260 270 280 DIQLQGIEDV ASAYTPVPGG VGPMTITTLI RQTVEAAEKA LA

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR543861 Genomic DNA. Translation: CAG69578.1.
RefSeq	YP_047400.1.
3D structure databases
HSSP	HSSP built from PDB template 1A4I based on UniProtKB P11586.
SMR	Q6F8N7. Positions 2-279.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6F8N7.
Genome annotation databases
GeneID	2878592.
GenomeReviews	Gene locus ACIAD2847 in contig CR543861_GR.
KEGG	aci:ACIAD2847.
NMPDR	fig|62977.3.peg.2593.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0190.
HOGENOM	HBG328751.
OMA	GPMTINT.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD2847-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. IPR020867. THF_DH/CycHdrlase_CS. IPR020631. THF_DH/CycHdrlase_NAD-bd_dom. [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.
PROSITE	PS00766. THF_DHG_CYH_1. False negative. PS00767. THF_DHG_CYH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLD2_ACIAD

Accession

Primary (citable) accession number: Q6F8N7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	July 19, 2004
Last modified:	January 19, 2010
This is version 37 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)