Reviewed, UniProtKB/Swiss-Prot Q0PA35 (FOLD_CAMJE)

Names and origin

Protein names

Recommended name:
    Bifunctional protein folD
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
Ordered Locus Names:	Cj0855

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	282 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 By similarity.
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 pathway. HAMAP MF_01576
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	methenyltetrahydrofolate cyclohydrolase activity Inferred from electronic annotation. Source: HAMAP methylenetetrahydrofolate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
fliM	Q0PC73	1	EBI-1191941,EBI-1191095
fliY	Q0PC74	1	EBI-1191941,EBI-1191111

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 282	282	Bifunctional protein folD HAMAP MF_01576		PRO_0000268304

Sequences

	Sequence		Length	Mass (Da)
	Q0PA35-1 [UniParc]. Last modified September 19, 2006. Version 1. Checksum: A692A4469F5B9AEB	FASTA	282	30,349
	10 20 30 40 50 60 MTLLDGKALS AKIKEELKEK NQFLKSKGIE SCLAVILVGD NPASQTYVKS KAKACEECGI 70 80 90 100 110 120 KSLVYHLNEN ITQNELLALI NTLNHDDSVH GILVQLPLPD HICKDLILES IISSKDVDGF 130 140 150 160 170 180 HPINVGYLNL GLESGFLPCT PLGVMKLLKA YEIDLEGKDA VIIGASNIVG RPMATMLLNA 190 200 210 220 230 240 GATVSVCHIK TKDLSLYTRQ ADLIIVAAGC VNLLRSDMVK EGVIVVDVGI NRLESGKIVG 250 260 270 280 DVDFEEVSKK SSYITPVPGG VGPMTIAMLL ENTVKSAKNR LN

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL111168 Genomic DNA. Translation: CAL34983.1.
PIR	G81358.
RefSeq	YP_002344262.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q0PA35. 37 interactions.
Genome annotation databases
GeneID	905155.
GenomeReviews	Gene locus Cj0855 in contig AL111168_GR.
KEGG	cje:Cj0855.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0PA35.
OMA	Q0PA35. HSKTRDL.
Enzyme and pathway databases
BRENDA	1.5.1.5. 255835. 3.5.4.9. 255835.
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_CAMJE

Accession

Primary (citable) accession number: Q0PA35

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	September 19, 2006
Last modified:	June 16, 2009
This is version 23 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)