[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=Sprague-Dawley; TISSUE=Liver; PubMed=1848231 [NCBI, ExPASy, EBI, Israel, Japan] Cook R.J., Lloyd R.S., Wagner C.; "Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase."; J. Biol. Chem. 266:4965-4973(1991).
[2]	PROTEIN SEQUENCE OF N-TERMINUS, AND MUTAGENESIS OF ASP-142. DOI=10.1074/jbc.274.50.35777; PubMed=10585460 [NCBI, ExPASy, EBI, Israel, Japan] Krupenko S.A., Wagner C.; "Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic centers of 10-formyltetrahydrofolate dehydrogenase."; J. Biol. Chem. 274:35777-35784(1999).
[3]	FUNCTION, AND SUBCELLULAR LOCATION. PubMed=3392008 [NCBI, ExPASy, EBI, Israel, Japan] Case G.L., Kaisaki P.J., Steele R.D.; "Resolution of rat liver 10-formyltetrahydrofolate dehydrogenase/hydrolase activities."; J. Biol. Chem. 263:10204-10207(1988).
[4]	MUTAGENESIS OF CYS-707, FUNCTION, AND SUBUNIT. DOI=10.1074/jbc.270.2.519; PubMed=7822273 [NCBI, ExPASy, EBI, Israel, Japan] Krupenko S.A., Wagner C., Cook R.J.; "Cysteine 707 is involved in the dehydrogenase activity site of rat 10-formyltetrahydrofolate dehydrogenase."; J. Biol. Chem. 270:519-522(1995).
[5]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr0503073; PubMed=16396499 [NCBI, ExPASy, EBI, Israel, Japan] Moser K., White F.M.; "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."; J. Proteome Res. 5:98-104(2006).
[6]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-309. DOI=10.1074/jbc.M313934200; PubMed=14729668 [NCBI, ExPASy, EBI, Israel, Japan] Chumanevich A.A., Krupenko S.A., Davies C.; "The crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase: mechanism of hydrolysis and its interplay with the dehydrogenase domain."; J. Biol. Chem. 279:14355-14364(2004).

Comments

CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + NADP⁺ + H₂O = tetrahydrofolate + CO₂ + NADPH.
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: In the N-terminal section; belongs to the GART family.
SIMILARITY: In the C-terminal section; belongs to the aldehyde dehydrogenase family. ALDH1L subfamily.
SIMILARITY: Contains 1 acyl carrier domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M59861; AAA70429.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A23709; A60560.

NP_071992.1; -.

3D structure databases

PDB

1S3I; X-ray; 2.30 A; A=1-309.	[ExPASy / RCSB / EBI]
2O2P; X-ray; 1.70 A; A/B/C/D=397-902.	[ExPASy / RCSB / EBI]
2O2Q; X-ray; 2.00 A; A/B/C/D=397-902.	[ExPASy / RCSB / EBI]
2O2R; X-ray; 2.20 A; A/B/C/D=397-902.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1S3I; -.
2O2P; -.
2O2Q; -.
2O2R; -.

P28037; 302-402.

PTM databases

P28037; -.

Organism-specific databases

RGD

621294; Fthfd.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0000036;	Molecular function: acyl carrier activity (inferred from electronic annotation from InterPro).
GO:0048037;	Molecular function: cofactor binding (inferred from electronic annotation from InterPro).
GO:0016155;	Molecular function: formyltetrahydrofolate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0016742;	Molecular function: hydroxymethyl-, formyl- and related transferase activity (inferred from electronic annotation from InterPro).
GO:0009258;	Biological process: 10-formyltetrahydrofolate catabolic process (inferred from electronic annotation from InterPro).
GO:0009058;	Biological process: biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006730;	Biological process: one-carbon compound metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR011407; 10_FTHF_DHase.
IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR005793; Formyl_trans_C.
IPR002376; Formyl_transf_N.
IPR001555; GART_AS.
IPR006163; Phsphopanteth_bd.
IPR006162; Ppantne_S.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
G3DSA:3.10.25.10; Formyl_trans_C; 1.
G3DSA:3.40.50.170; Formyl_transf_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.

Pfam

PF00171; Aldedh; 1.
PF02911; Formyl_trans_C; 1.
PF00551; Formyl_trans_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036489; 10-FTHFDH; 1.

PROSITE

PS50075; ACP_DOMAIN; 1.
PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PS00373; GART; 1.
PS00012; PHOSPHOPANTETHEINE; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P28037.

Genome annotation databases

GeneID

64392; -.

KEGG

rno:64392; -.

Phylogenomic databases

HOVERGEN

P28037; -.

Other

NextBio

613150; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Direct protein sequencing; NADP; One-carbon metabolism; Oxidoreductase; Phosphopantetheine; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 902`	`902`	`10-formyltetrahydrofolate dehydrogenase.`	`PRO_0000199422`
`DOMAIN`	`323 392`	`70`	`Acyl carrier.`
`REGION`	`1 203`	`203`	`GART.`
`REGION`	`417 902`	`486`	`Aldehyde dehydrogenase.`
`ACT_SITE`	`106 106`		`Proton donor (By similarity).`
`ACT_SITE`	`673 673`		`By similarity.`
`ACT_SITE`	`707 707`		`Probable.`
`BINDING`	`354 354`		`Phosphopantetheine (covalent) (By similarity).`
`SITE`	`142 142`	`1`	`Essential for catalytic activity (By similarity).`
`MOD_RES`	`354 354`		`Phosphoserine.`
`MUTAGEN`	`142 142`		`D->A,N,E,Q: Loss of hydrolase activity.`
`MUTAGEN`	`707 707`		`C->A: Loss of dehydrogenase activity. No effect on hydrolase activity and NADP binding.`
`STRAND`	`2 7`	`6`
`HELIX`	`10 21`	`12`
`STRAND`	`25 30`	`6`
`HELIX`	`41 49`	`9`
`STRAND`	`59 61`	`3`
`HELIX`	`67 74`	`8`
`STRAND`	`79 85`	`7`
`HELIX`	`92 95`	`4`
`STRAND`	`96 98`	`3`
`STRAND`	`102 108`	`7`
`TURN`	`110 113`	`4`
`STRAND`	`114 116`	`3`
`HELIX`	`118 124`	`7`
`STRAND`	`128 136`	`9`
`STRAND`	`139 142`	`4`
`STRAND`	`146 153`	`8`
`HELIX`	`160 166`	`7`
`HELIX`	`168 185`	`18`
`HELIX`	`206 209`	`4`
`STRAND`	`213 215`	`3`
`HELIX`	`217 225`	`9`
`TURN`	`226 231`	`6`
`STRAND`	`233 237`	`5`
`STRAND`	`240 249`	`10`
`STRAND`	`258 260`	`3`
`STRAND`	`271 273`	`3`
`STRAND`	`276 280`	`5`
`STRAND`	`286 294`	`9`
`STRAND`	`299 301`	`3`
`HELIX`	`302 304`	`3`
`STRAND`	`409 413`	`5`
`STRAND`	`416 420`	`5`
`STRAND`	`423 426`	`4`
`STRAND`	`429 431`	`3`
`HELIX`	`434 436`	`3`
`STRAND`	`438 442`	`5`
`TURN`	`444 446`	`3`
`STRAND`	`449 454`	`6`
`HELIX`	`458 473`	`16`
`HELIX`	`476 478`	`3`
`HELIX`	`482 498`	`17`
`HELIX`	`500 511`	`12`
`HELIX`	`515 520`	`6`
`TURN`	`521 523`	`3`
`HELIX`	`524 536`	`13`
`HELIX`	`537 539`	`3`
`STRAND`	`542 545`	`4`
`STRAND`	`553 563`	`11`
`STRAND`	`566 570`	`5`
`STRAND`	`573 575`	`3`
`HELIX`	`576 589`	`14`
`STRAND`	`593 597`	`5`
`HELIX`	`604 615`	`12`
`STRAND`	`622 625`	`4`
`HELIX`	`630 639`	`10`
`STRAND`	`645 650`	`6`
`HELIX`	`652 664`	`13`
`STRAND`	`669 673`	`5`
`STRAND`	`678 682`	`5`
`HELIX`	`688 700`	`13`
`HELIX`	`701 704`	`4`
`STRAND`	`710 716`	`7`
`HELIX`	`717 731`	`15`
`HELIX`	`752 767`	`16`
`STRAND`	`771 774`	`4`
`STRAND`	`780 783`	`4`
`STRAND`	`789 793`	`5`
`HELIX`	`799 801`	`3`
`STRAND`	`807 815`	`9`
`HELIX`	`821 827`	`7`
`STRAND`	`837 839`	`3`
`HELIX`	`843 852`	`10`
`STRAND`	`855 861`	`7`
`HELIX`	`876 878`	`3`
`HELIX`	`885 890`	`6`

Sequence information

Length: 902 AA [This is the length of the unprocessed precursor]

Molecular weight: 99127 Da [This is the MW of the unprocessed precursor]

CRC64: C8BB2418357FF6FE [This is a checksum on the sequence]

        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

P28037 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools