Reviewed, UniProtKB/Swiss-Prot Q74J95 (FOLD1_LACJO)

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:	LJ_1215

Organism

Lactobacillus johnsonii [Complete proteome] [HAMAP]

Taxonomic identifier

33959 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	283 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 – 283	283	Bifunctional protein folD 1 HAMAP MF_01576		PRO_0000268375

Sequences

	Sequence		Length	Mass (Da)
	Q74J95-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 4CE5798DAE57CF18	FASTA	283	31,279
	10 20 30 40 50 60 MTNIINGRQI AKQLNQETKT RVDKLKEEGI IPGIVVILVG DDPASVIYTR NKQKNAEKLG 70 80 90 100 110 120 MKSILRKFPK DVSQAEVLQA IHHYNDDPTI HAILIQLPLP KHLNQTELIE AIAPEKDVDG 130 140 150 160 170 180 FNSKNVGKLY NNEEGHYPVS CTSRGIMTLL HTYLDKIEGL NVTIVGRSIL VSRPLQSLLI 190 200 210 220 230 240 NENATVTMVS LHTDNIDYYT KHADILVVAA GKPNLIKKDQ VKPGATVIDV GINRMANHYL 250 260 270 280 VGDVDFDDVK EVAKNITPVP GGVGPMTIAT LMQQTVDLAE WNK

References

[1]

"The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533." Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C., Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R., Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A. Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004) [PubMed: 14983040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCC 533.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017198 Genomic DNA. Translation: AAS09036.1.
RefSeq	NP_965070.1.
3D structure databases
HSSP	HSSP built from PDB template 1A4I based on UniProtKB P11586.
SMR	Q74J95. Positions 2-281.
ModBase	Search...
Genome annotation databases
GeneID	2743234.
GenomeReviews	Gene locus LJ_1215 in contig AE017198_GR.
KEGG	ljo:LJ1215.
NMPDR	fig|257314.1.peg.1056.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG328751.
OMA	DVVYETA.
Enzyme and pathway databases
BioCyc	LJOH257314:LJ_1215-MONOMER.
BRENDA	1.5.1.5. 141476. 3.5.4.9. 141476.
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. 1 hit. PS00767. THF_DHG_CYH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLD1_LACJO

Accession

Primary (citable) accession number: Q74J95

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	July 5, 2004
Last modified:	January 19, 2010
This is version 38 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)