10-formyltetrahydrofolate dehydrogenase

Contribute

Send feedback

Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot O75891 (FTHFD_HUMAN)

Last modified June 16, 2009. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

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

Hide | Top

Names and origin

Protein names

Recommended name:
    10-formyltetrahydrofolate dehydrogenase
      Short name=10-FTHFDH
    EC=1.5.1.6
Alternative name(s):
    Aldehyde dehydrogenase family 1 member L1

Gene names

Name:	ALDH1L1
Synonyms:	FTHFD

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	902 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity

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

Subcellular location

Cytoplasm.

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.

Hide | Top

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	NADP Phosphopantetheine
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	10-formyltetrahydrofolate catabolic process Traceable author statement. Source: ProtInc biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon compound metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acyl carrier activity Inferred from electronic annotation. Source: InterPro formyltetrahydrofolate dehydrogenase activity Inferred from electronic annotation. Source: EC hydroxymethyl-, formyl- and related transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 902

902

10-formyltetrahydrofolate dehydrogenase

PRO_0000199419

Regions

Domain

323 – 392

Acyl carrier

Region

1 – 203

203

GART

Region

417 – 902

486

Aldehyde dehydrogenase

Sites

Active site

106

Proton donor By similarity

Active site

673

By similarity

Active site

707

By similarity

Site

142

Essential for catalytic activity By similarity

Amino acid modifications

Modified residue

354

O-(pantetheine 4'-phosphoryl)serine By similarity

Natural variations

Natural variant

254

L → P: dbSNP rs3796191.

VAR_052290

Natural variant

330

V → F: dbSNP rs2886059.

VAR_052291

Natural variant

429

E → A: dbSNP rs9282691.

VAR_052292

Natural variant

436

A → T: dbSNP rs9282692.

VAR_052293

Natural variant

436

A → V: dbSNP rs9282693.

VAR_052294

Natural variant

448

S → N: dbSNP rs9282697.

VAR_052295

Natural variant

481

S → G: dbSNP rs2276724.

VAR_052296

Natural variant

511

A → V in a colorectal cancer sample; somatic mutation. Ref.5

VAR_036101

Natural variant

793

D → G: dbSNP rs1127717.

VAR_052297

Natural variant

803

E → K: dbSNP rs9282689.

VAR_052298

Natural variant

812

I → V: dbSNP rs4646750.

VAR_052299

Experimental info

Sequence conflict

G → A in AAC35000. Ref.1

Sequence conflict

F → S in AAC35000. Ref.1

Sequence conflict

176

M → V in AAC35000. Ref.1

Sequence conflict

195

E → K in AAC35000. Ref.1

Sequence conflict

470

D → G in AAC35000. Ref.1

Sequence conflict

677

K → E in AAC35000. Ref.1

Sequence conflict

680

L → F in AAC35000. Ref.1

Sequence conflict

702

N → S in AAC35000. Ref.1

Secondary structure

902

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

O75891-1 [UniParc].

Last modified February 15, 2005. Version 2.
Checksum: D92CB2930617F7CF
Show »

FASTA

902

98,829

        10         20         30         40         50         60 
MKIAVIGQSL FGQEVYCHLR KEGHEVVGVF TVPDKDGKAD PLGLEAEKDG VPVFKYSRWR 

        70         80         90        100        110        120 
AKGQALPDVV AKYQALGAEL NVLPFCSQFI PMEIISAPRH GSIIYHPSLL PRHRGASAIN 

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

       190        200        210        220        230        240 
RLIAEGKAPR LPQPEEGATY EGIQKKETAK INWDQPAEAI HNWIRGNDKV PGAWTEACEQ 

       250        260        270        280        290        300 
KLTFFNSTLN TSGLVPEGDA LPIPGAHRPG VVTKAGLILF GNDDKMLLVK NIQLEDGKMI 

       310        320        330        340        350        360 
LASNFFKGAA SSVLELTEAE LVTAEAVRSV WQRILPKVLE VEDSTDFFKS GAASVDVVRL 

       370        380        390        400        410        420 
VEEVKELCDG LELENEDVYM ASTFGDFIQL LVRKLRGDDE EGECSIDYVE MAVNKRTVRM 

       430        440        450        460        470        480 
PHQLFIGGEF VDAEGAKTSE TINPTDGSVI CQVSLAQVTD VDKAVAAAKD AFENGRWGKI 

       490        500        510        520        530        540 
SARDRGRLMY RLADLMEQHQ EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI 

       550        560        570        580        590        600 
QGSTIPINQA RPNRNLTLTR KEPVGVCGII IPWNYPLMML SWKTAACLAA GNTVVIKPAQ 

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

       670        680        690        700        710        720 
SCAISNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF FNKGENCIAA GRLFVEDSIH 

       730        740        750        760        770        780 
DEFVRRVVEE VRKMKVGNPL DRDTDHGPQN HHAHLVKLME YCQHGVKEGA TLVCGGNQVP 

       790        800        810        820        830        840 
RPGFFFEPTV FTDVEDHMFI AKEESFGPVM IISRFADGDL DAVLSRANAT EFGLASGVFT 

       850        860        870        880        890        900 
RDINKALYVS DKLQAGTVFV NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRVKTVTF 


EY

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Hong M.H., Lee Y., Kim J.W., Kang B.S., Choe I.S. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon carcinoma.
[3]	"Crystal structure of human 10-formyltetrahydrofolate dehydrogenase." Ogg D.J., Stenmark P., Arrowsmith C., Edwards A., Ehn M., Graslund S., Hammarstrom M., Hallberg M., Kotenyova T., Nilsson-Ehle P., Nordlund P., Persson C., Sagemark J., Schuler H., Sundstrom M., Thorsell A., Weigelt J. Submitted (JUL-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-307.
[4]	"Solution structure of RSGI RUH-033, a PP-binding domain of 10-FTHFDH from human cDNA." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 303-405.
[5]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-511.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

AF052732 mRNA. Translation: AAC35000.1.
CR749807 mRNA. Translation: CAH18667.1. Different initiation.

IPI

IPI00290553.

RefSeq

NP_036322.2.

UniGene

Hs.434435

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BW0	X-ray	1.70	A	1-307	[»]
2CFI	X-ray	1.85	A	1-307	[»]
2CQ8	NMR	-	A	305-401	[»]

SMR

O75891. Positions 406-902.

ModBase

Search...

PTM databases

PhosphoSite

O75891.

Proteomic databases

PRIDE

O75891.

Genome annotation databases

Ensembl

ENSG00000144908. Homo sapiens. [Contig view]

GeneID

10840.

KEGG

hsa:10840.

NMPDR

fig|9606.3.peg.23112.

Organism-specific databases

GeneCards

GC03M127306.

HGNC

HGNC:3978. ALDH1L1.

MIM

600249. gene.

PharmGKB

PA28393.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O75891.

Enzyme and pathway databases

BRENDA

1.5.1.6. 247.

Gene expression databases

ArrayExpress

O75891.

Bgee

O75891.

CleanEx

HS_ALDH1L1.

GermOnline

ENSG00000144908. Homo sapiens.

Family and domain databases

InterPro

IPR011407. 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]

Gene3D

G3DSA: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.

PANTHER

PTHR11699. Aldehyde_dehyd. 1 hit.

Pfam

PF00171. Aldedh. 1 hit.
PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]

PIRSF

PIRSF036489. 10-FTHFDH. 1 hit.

PROSITE

PS50075. 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]

ProtoNet

Search...

Other Resources

DrugBank

DB00116. Tetrahydrofolic acid.

NextBio

41156.

SOURCE

Search...

Hide | Top

Entry information

Entry name

FTHFD_HUMAN

Accession

Primary (citable) accession number: O75891
Secondary accession number(s): Q68CS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 15, 2005
Last modified:	June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top