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Q9ZD32 (FOLD_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismRickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceInferred 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-Rule MF_01576

Catalytic activity

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH. HAMAP-Rule MF_01576

5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. HAMAP-Rule MF_01576

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_01576

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01576

Sequence similarities

Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

Sequence caution

The sequence CAA14967.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286Bifunctional protein FolD HAMAP-Rule MF_01576
PRO_0000199314

Regions

Nucleotide binding167 – 1693NADP By similarity

Sites

Binding site1921NADP By similarity
Binding site2331NADP; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZD32 [UniParc].

Last modified October 11, 2004. Version 2.
Checksum: 118DE987C14D857B

FASTA28630,560
        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 

« Hide

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] [Europe PMC] [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.
PIRE71655.
RefSeqNP_220891.1. NC_000963.1.

3D structure databases

ProteinModelPortalQ9ZD32.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272947.RP515.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA14967; CAA14967; CAA14967.
GeneID883180.
KEGGrpr:RP515.
PATRIC17901816. VBIRicPro72556_0526.

Phylogenomic databases

eggNOGCOG0190.
HOGENOMHOG000218242.
KOK01491.
OrthoDBEOG6K6VBB.
ProtClustDBPRK14171.

Enzyme and pathway databases

UniPathwayUPA00193.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_01576. THF_DHG_CYH.
InterProIPR016040. 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]
PfamPF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSPR00085. THFDHDRGNASE.
PROSITEPS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFOLD_RICPR
AccessionPrimary (citable) accession number: Q9ZD32
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways