[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Embryo; NIH - Xenopus Gene Collection (XGC) project; Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + NADP⁺ + H₂O = tetrahydrofolate + CO₂ + NADPH.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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

BC073490; AAH73490.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001085894.1; -.

UniGene

Xl.5930

3D structure databases

SMR

Q6GNL7; 1-307, 405-902.

ModBase

Q6GNL7.

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).

BLOCKS

Q6GNL7.

Genome annotation databases

GeneID

444321; -.

KEGG

xla:444321; -.

Phylogenomic databases

HOVERGEN

Q6GNL7; -.

Other

ProtoNet

Q6GNL7.

UniRef

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

Keywords

Cytoplasm; NADP; One-carbon metabolism; Oxidoreductase; Phosphopantetheine.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 902`	`902`	`10-formyltetrahydrofolate dehydrogenase.`	`PRO_0000315999`
`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`		`By similarity.`
`BINDING`	`354 354`		`Phosphopantetheine (covalent) (By similarity).`
`SITE`	`142 142`	`1`	`Essential for catalytic activity (By similarity).`

Sequence information

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

Molecular weight: 99982 Da [This is the MW of the unprocessed precursor]

CRC64: C484728096D4C281 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIAVIGQSL FGREVYRELL KEGHQVVGVF TIPDKNGKAD PLGADAEKDG IPVFKFPRWR 

        70         80         90        100        110        120 
VKGQAIPEVV EKYKALEAEL NVLPFCSQFI PMEVIDCPKH GSIIYHPSIL PRHRGASAIN 

       130        140        150        160        170        180 
WTLMQGDKIG GFTVFWADDG LDTGDILLQR QCEVLPDDTV NTIYNRFLFP EGVKGMVEAV 

       190        200        210        220        230        240 
RLIAEGNAPR IKQPTEGATY DPMQKKENAK INWDQPAEDI HNFIRGNDKV PGAWTVVDDQ 

       250        260        270        280        290        300 
QLTFFGSSFT RNGPAPDGQP LEIPGASRPA LVTKTGLVLF GNDGERLTVK NIQFEDGKMI 

       310        320        330        340        350        360 
PASQYFKTAD SAALQLSEEE QKVSEEIRAA WRRILTNVSE IEDSTDFFKA GAASMDVVRL 

       370        380        390        400        410        420 
VEEVKLKCNG LQLQNEDVYM ATKFEEFIQM VVRRMRGEDG EEELVIDYVE KEINNMTVKI 

       430        440        450        460        470        480 
PHQLFINGQF MDAEGGKSYD TINPTDGTAI CKVSLAQISD IDRAVAAAKE AFENGEWGKM 

       490        500        510        520        530        540 
NPRDRGRLLY RLADLMEEHQ EELATIESID SGAVYTLALK THVGMSIQTF RYFAGWCDKI 

       550        560        570        580        590        600 
QGRTIPINQA RPNRNLTFTR REPIGVCGIV IPWNYPLMML AWKTAACLTA GNTVVLKPAQ 

       610        620        630        640        650        660 
VTPLTALKFA ELSVKAGIPK GVINILPGAG SLIGQRLSDH PDVRKIGFTG STPIGKQIMK 

       670        680        690        700        710        720 
SCAVSNVKKV SLELGGKSPL IIFHDCDLDK AVRMGMSSVF FNKGENCIAA GRLFLEESIH 

       730        740        750        760        770        780 
DEFVKRVVEE VKKMKIGDPL DRSTDHGPQN HKAHLDKLIE YCQTGVKEGG KLVYGGKQVE 

       790        800        810        820        830        840 
RPGFFFEPTI FTDVTDEMFI AKEESFGPVM IISKFNDGDI DGVLKRANDS EFGLASGVFT 

       850        860        870        880        890        900 
KDINKALYVS EKLQAGTVFV NTYNKTDVAA PFGGFKQSGF GKDLGEEALN EYLKTKAVTI 


EY

Q6GNL7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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