Reviewed, UniProtKB/Swiss-Prot P51696 (FOLD_PHOPO)

Names and origin

Protein names

Recommended name:
    Bifunctional protein folD
Alternative name(s):
    PPDC
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:

folD

Organism

Photobacterium phosphoreum

Taxonomic identifier

659 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Photobacterium

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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. 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
Enzyme regulation	The NAD+-dependent dehydrogenase is activated by inorganic phosphate. HAMAP MF_01576
Pathway	One-carbon metabolism; tetrahydrofolate pathway. HAMAP MF_01576
Subunit structure	Homodimer. HAMAP MF_01576
Sequence similarities	Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
biophysicochemical properties	Kinetic parameters: KM=0.20 mM for NADP+ HAMAP MF_01576 KM=4.76 mM for NAD+

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis Methionine biosynthesis One-carbon metabolism Purine biosynthesis
Ligand	NADP
Molecular function	Hydrolase Oxidoreductase
Technical term	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 – 285	285	Bifunctional protein folD HAMAP MF_01576		PRO_0000199312

Sequences

	Sequence		Length	Mass (Da)
	P51696-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 9EB1FC954EAA4396	FASTA	285	30,776
	10 20 30 40 50 60 MSAQIIDGKI ISQTVRQEVA ARVKARTDAG LRAPGLAVVL VGQDPASQIY VGSKRKACEE 70 80 90 100 110 120 VGFISKSFDL PSSASEQQLL DLIDELNQDP TMDGILVQLP LPAGMDCTRI LERIDPEKDV 130 140 150 160 170 180 DGFHPYNVGR LSQRIPKLRS CTPKGIITLL ERYNIEVRGK HAVIVGASNI VGRPMTLELL 190 200 210 220 230 240 LAGATTTTCH RFTQDLEGHI RQADILVVAV GKPNFIPGGW IKEGATVIDV GINRLENGKL 250 260 270 280 CGDVEFDVAC QRAKYITPVP GGVGPMTVAS LIENTLLACE QYHSA

References

[1]

"Methylenetetrahydrofolate dehydrogenase-cyclohydrolase from Photobacterium phosphoreum shares properties with a mammalian mitochondrial homologue." Pawelek P.D., MacKenzie R.E. Biochim. Biophys. Acta 1296:47-54(1996) [PubMed: 8765228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: DSM 2167 / LMG 4231 / NCIMB 844.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U34207 Genomic DNA. Translation: AAA98507.1.
PIR	S71924.
3D structure databases
HSSP	HSSP built from PDB template 1B0A based on UniProtKB P24186.
SMR	P51696. Positions 2-283.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.5.1.5. 348. 3.5.4.9. 348.
Family and domain databases
HAMAP	MF_01576. [Tree]
InterPro	IPR016040. NAD(P)-bd_dom. IPR000672. THF_DH/CycHdrlase. [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

FOLD_PHOPO

Accession

Primary (citable) accession number: P51696

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 49 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)