Reviewed, UniProtKB/Swiss-Prot Q88KM5 (FOLD2_PSEPK)

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
Synonyms:	folD-2
Ordered Locus Names:	PP_2265

Organism

Pseudomonas putida (strain KT2440) [Complete proteome] [HAMAP]

Taxonomic identifier

160488 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	284 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 – 284	284	Bifunctional protein folD 2		PRO_0000268447

Sequences

	Sequence		Length	Mass (Da)
	Q88KM5-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: BB4DD5666732B193	FASTA	284	30,623
	10 20 30 40 50 60 MTAHLIDGKA IAASLRQQIA QRVVERRQQG LRTPGLAVIL VGTDPASQVY VSHKRKDCEE 70 80 90 100 110 120 VGFISQAFDL PSETTQQALT ELIDRLNDDP AVDGILLQLP LPAHLDASLL LERIRPDKDV 130 140 150 160 170 180 DGFHPYNIGR LAQRIPLLRP CTPKGIMTLL ESTGQDLYGM NAVIVGASNI VGRPMAMELL 190 200 210 220 230 240 LAGCTVTVCH RFTKDLAGHV GRADLVVVAA GKPGLVKGEW VKEGAIVIDV GINRQEDGKL 250 260 270 280 VGDVVYETAL PRAGWITPVP GGVGPMTRAC LLENTLYAAE ELHK

References

[1]

"Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440." Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M., Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F., Madupu R., Nelson W.C., White O. , Peterson J.D., Khouri H.M., Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M. Environ. Microbiol. 4:799-808(2002) [PubMed: 12534463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE015451 Genomic DNA. Translation: AAN67878.1.
RefSeq	NP_744414.1.
3D structure databases
HSSP	HSSP built from PDB template 1B0A based on UniProtKB P24186.
ModBase	Search...
Genome annotation databases
GeneID	1045158.
GenomeReviews	Gene locus PP_2265 in contig AE015451_GR.
KEGG	ppu:PP_2265.
NMPDR	fig|160488.1.peg.2244.
TIGR	PP_2265.
Phylogenomic databases
HOGENOM	Q88KM5.
Enzyme and pathway databases
BioCyc	PPUT160488:PP_2265-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

FOLD2_PSEPK

Accession

Primary (citable) accession number: Q88KM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	June 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)