Q9ZD32 (FOLD_RICPR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional protein FolD

Including the following 2 domains:

1. Methylenetetrahydrofolate dehydrogenase
   EC=1.5.1.5
2. Methenyltetrahydrofolate cyclohydrolase
   EC=3.5.4.9

Gene names

Name:	folD
Ordered Locus Names:	RP515

Organism

Rickettsia prowazekii (strain Madrid E)

Taxonomic identifier

272947 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group

Protein attributes

Sequence length	286 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.
Sequence caution	The sequence CAA14967.1 differs from that shown. Reason: Erroneous initiation.

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 Reference proteome
Gene Ontology (GO)
Biological process	folic acid-containing compound 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 purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	methenyltetrahydrofolate cyclohydrolase activity Inferred from electronic annotation. Source: EC methylenetetrahydrofolate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 286	286	Bifunctional protein FolD HAMAP MF_01576		PRO_0000199314

Sequences

	Sequence		Length	Mass (Da)
	Q9ZD32 [UniParc]. Last modified October 11, 2004. Version 2. Checksum: 118DE987C14D857B	FASTA	286	30,560
	10 20 30 40 50 60 MVNNIIDGKA LANEILADLK LEIQGFKEKT KTSPKLAIVL VGDNPASMIY VKNKIKNAHQ 70 80 90 100 110 120 VGIDTLLVNL STNIYTDDLI LKINELNLDK GISGIIVQLP LPSSIDENKI LSAVLPSKDS 130 140 150 160 170 180 DGFHPLNVGY LHSGINQGFI PCTALGCLAV IKKYAPNLNG KDAVIVGRSN IVGKPLSALL 190 200 210 220 230 240 LQENCSVTIC HSKTCNLSSI TSKADIVVVA IGSPLKLTAE YFNPEAIVID VGINRISHNK 250 260 270 280 IAGDVDFENV KSKVKYITPV PGGIGPMTIA FLLKNTVKAF KNAIAL

References

[1]

"The genome sequence of Rickettsia prowazekii and the origin of mitochondria." Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G. Nature 396:133-140(1998) [PubMed: 9823893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Madrid E.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ235272 Genomic DNA. Translation: CAA14967.1. Different initiation.
PIR	E71655.
RefSeq	NP_220891.1. NC_000963.1.
3D structure databases
ProteinModelPortal	Q9ZD32.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	883180.
GenomeReviews	Gene locus RP515 in contig AJ235269_GR.
KEGG	rpr:RP515.
PATRIC	17901816. VBIRicPro72556_0526.
Phylogenomic databases
HOGENOM	HBG328751.
ProtClustDB	PRK14171.
Enzyme and pathway databases
BioCyc	RPRO272947:RP515-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.
KO	K01491.
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

FOLD_RICPR

Accession

Primary (citable) accession number: Q9ZD32

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2001
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program