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Reviewed, UniProtKB/Swiss-Prot P28037 (FTHFD_RAT)

Last modified June 16, 2009. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    10-formyltetrahydrofolate dehydrogenase
      Short name=10-FTHFDH
    EC=1.5.1.6
Alternative name(s):
    Aldehyde dehydrogenase family 1 member L1
    FBP-CI
Gene names
Name: Aldh1l1
Synonyms: Fthfd
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length902 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH.

Subunit structure

Homotetramer. Ref.4

Subcellular location

Cytoplasm. Ref.3

Sequence similarities

In the N-terminal section; belongs to the GART family.

In the C-terminal section; belongs to the aldehyde dehydrogenase family. ALDH1L subfamily.

Contains 1 acyl carrier domain.

Caution

The phosphoserine observed at Ser-354 in Ref.5 undoubtedly results from the secondary neutral loss of pantetheine from the phosphodiester linked cofactor.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 90290210-formyltetrahydrofolate dehydrogenase
PRO_0000199422

Regions

Domain323 – 39270Acyl carrier
Region1 – 203203GART
Region417 – 902486Aldehyde dehydrogenase

Sites

Active site1061Proton donor By similarity
Active site6731 By similarity
Active site7071 Probable
Site1421Essential for catalytic activity By similarity

Amino acid modifications

Modified residue3541O-(pantetheine 4'-phosphoryl)serine Probable

Experimental info

Mutagenesis1421D → A, N, E or Q: Loss of hydrolase activity. Ref.2
Mutagenesis7071C → A: Loss of dehydrogenase activity. No effect on hydrolase activity and NADP binding. Ref.4

Secondary structure

1 ............................................................................................................................................. 902
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P28037-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: C8BB2418357FF6FE

FASTA90299,127
        10         20         30         40         50         60 
MKIAVIGQSL FGQEVYCQLR KEGHEVVGVF TIPDKDGKAD PLGLEAEKDG RAVFKFPRWR 

        70         80         90        100        110        120 
ARGQALPEVV AKYQALGAEL NVLPFCSQFI PMEVINAPRH GSIIYHPSLL PRHRGASAIN 

       130        140        150        160        170        180 
WTLIHGDKKG GFTIFWADDG LDTGDLLLQK ECEVLPDDTV STLYNRFLFP EGIKGMVQAV 

       190        200        210        220        230        240 
RLIAEGTAPR CPQSEEGATY EGIQKKETAK INWDQPAEAI HNWIRGNDKV PGAWTEACGQ 

       250        260        270        280        290        300 
KLTFFNSTLN TSGLSTQGEA LPIPGAHRPG VVTKAGLILF GNEHRMLLVK NIQLEDGKMM 

       310        320        330        340        350        360 
PASQFFKGSA SSDLELTEAE LATAEAVRSS WMRILPNVPE VEDSTDFFKS GAASVDVVRL 

       370        380        390        400        410        420 
VEEVKELCDG LELENEDVYM ATTFREFIQL LVRKLRGEDD ESECVINYVE RAVNKLTLQM 

       430        440        450        460        470        480 
PYQLFIGGEF VDAEGSKTYN TINPTDGSVI CQVSLAQVSD VDKAVAAAKE AFENGLWGKI 

       490        500        510        520        530        540 
NARDRGRLLY RLADVMEQHQ EELATIEALD RGAVYTLALK THVGMSIQTF RYFAGWCDKI 

       550        560        570        580        590        600 
QGATIPINQA RPNRNLTLTK KEPVGVCGIV IPWNYPLMML SWKTAACLAA GNTVVIKPAQ 

       610        620        630        640        650        660 
VTPLTALKFA ELTLKAGIPK GVVNILPGSG SLVGQRLSDH PDVRKIGFTG STEVGKHIMK 

       670        680        690        700        710        720 
SCALSNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF FNKGENCIAA GRLFVEESIH 

       730        740        750        760        770        780 
NQFVQKVVEE VEKMKIGNPL ERDTNHGPQN HEAHLRKLVE YCQRGVKEGA TLVCGGNQVP 

       790        800        810        820        830        840 
RPGFFFQPTV FTDVEDHMYI AKEESFGPIM IISRFADGDV DAVLSRANAT EFGLASGVFT 

       850        860        870        880        890        900 
RDINKALYVS DKLQAGTVFI NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRIKTVTF 


EY

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References

« Hide 'large scale' references
[1]"Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase."
Cook R.J., Lloyd R.S., Wagner C.
J. Biol. Chem. 266:4965-4973(1991) [PubMed: 1848231] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic centers of 10-formyltetrahydrofolate dehydrogenase."
Krupenko S.A., Wagner C.
J. Biol. Chem. 274:35777-35784(1999) [PubMed: 10585460] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, MUTAGENESIS OF ASP-142.
[3]"Resolution of rat liver 10-formyltetrahydrofolate dehydrogenase/hydrolase activities."
Case G.L., Kaisaki P.J., Steele R.D.
J. Biol. Chem. 263:10204-10207(1988) [PubMed: 3392008] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[4]"Cysteine 707 is involved in the dehydrogenase activity site of rat 10-formyltetrahydrofolate dehydrogenase."
Krupenko S.A., Wagner C., Cook R.J.
J. Biol. Chem. 270:519-522(1995) [PubMed: 7822273] [Abstract]
Cited for: MUTAGENESIS OF CYS-707, FUNCTION, SUBUNIT.
[5]"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."
Moser K., White F.M.
J. Proteome Res. 5:98-104(2006) [PubMed: 16396499] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, MASS SPECTROMETRY.
Tissue: Liver.
[6]"The crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase: mechanism of hydrolysis and its interplay with the dehydrogenase domain."
Chumanevich A.A., Krupenko S.A., Davies C.
J. Biol. Chem. 279:14355-14364(2004) [PubMed: 14729668] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-309.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M59861 mRNA. Translation: AAA70429.1.
IPIIPI00196725.
PIRA60560. A23709.
RefSeqNP_071992.1.
UniGeneRn.2328

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1S3IX-ray2.30A1-309[»]
2O2PX-ray1.70A/B/C/D397-902[»]
2O2QX-ray2.00A/B/C/D397-902[»]
2O2RX-ray2.20A/B/C/D397-902[»]
SMRP28037. Positions 302-402.
ModBaseSearch...

PTM databases

PhosphoSiteP28037.

Proteomic databases

PRIDEP28037.

Genome annotation databases

GeneID64392.
KEGGrno:64392.

Organism-specific databases

RGD621294. Fthfd.

Phylogenomic databases

HOVERGENP28037.

Enzyme and pathway databases

BRENDA1.5.1.6. 248.

Family and domain databases

InterProIPR011407. 10_FTHF_DH.
IPR009081. Acyl_carrier_prot-like.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR001555. GART_AS.
IPR006162. Ppantne_S.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
G3DSA:3.10.25.10. Formyl_trans_C. 1 hit.
G3DSA:3.40.50.170. Formyl_transf_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF00171. Aldedh. 1 hit.
PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
PIRSFPIRSF036489. 10-FTHFDH. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
PS00373. GART. 1 hit.
PS00012. PHOSPHOPANTETHEINE. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio613150.

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Entry information

Entry nameFTHFD_RAT
AccessionPrimary (citable) accession number: P28037
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1996
Last modified: June 16, 2009
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents