ID F6PXK1_CALJA Unreviewed; 911 AA.
AC F6PXK1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=10-formyltetrahydrofolate dehydrogenase {ECO:0000256|PIRNR:PIRNR036489};
DE EC=1.5.1.6 {ECO:0000256|PIRNR:PIRNR036489};
GN Name=ALDH1L1 {ECO:0000313|Ensembl:ENSCJAP00000012817.5};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000012817.5, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000012817.5}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000012817.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-10-formyltetrahydrofolate + H2O + NADP(+) = (6S)-5,6,7,8-
CC tetrahydrofolate + CO2 + H(+) + NADPH; Xref=Rhea:RHEA:10180,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:195366; EC=1.5.1.6;
CC Evidence={ECO:0000256|ARBA:ARBA00036910};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10181;
CC Evidence={ECO:0000256|ARBA:ARBA00036910};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC dehydrogenase family. ALDH1L subfamily. {ECO:0000256|ARBA:ARBA00007995,
CC ECO:0000256|PIRNR:PIRNR036489}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the GART family.
CC {ECO:0000256|ARBA:ARBA00010978, ECO:0000256|PIRNR:PIRNR036489}.
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DR AlphaFoldDB; F6PXK1; -.
DR Ensembl; ENSCJAT00000013509.5; ENSCJAP00000012817.5; ENSCJAG00000006865.5.
DR eggNOG; KOG2452; Eukaryota.
DR GeneTree; ENSGT00940000160913; -.
DR TreeFam; TF354242; -.
DR Proteomes; UP000008225; Chromosome 15.
DR Bgee; ENSCJAG00000006865; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd07140; ALDH_F1L_FTFDH; 1.
DR CDD; cd08703; FDH_Hydrolase_C; 1.
DR CDD; cd08647; FMT_core_FDH_N; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.10.25.10; Formyl transferase, C-terminal domain; 1.
DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR InterPro; IPR011407; 10_FTHF_DH.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR037022; Formyl_trans_C_sf.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR001555; GART_AS.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR11699:SF120; CYTOSOLIC 10-FORMYLTETRAHYDROFOLATE DEHYDROGENASE; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF036489; 10-FTHFDH; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00373; GART; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR036489};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|PIRNR:PIRNR036489};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR036489,
KW ECO:0000256|RuleBase:RU003345};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT DOMAIN 327..404
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 682
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 682
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 716
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT BINDING 97..99
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 151
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 580..582
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 606..609
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 639..644
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 659..660
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 766
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 813..815
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT SITE 151
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-4"
SQ SEQUENCE 911 AA; 99858 MW; 8BD293FD71307A6D CRC64;
MGPSNHPTAM KIAVIGQSLF GQEVYCHLRK EGHEVVGVFT VPDKDGKADP LGLQAEKDGV
PVFKFARWRA KGQVLPDVVA KYQALGAELN VLPFCSQFIP MEIINAPRHG SIIYHPSLLP
RHRGASAINW TLIHGDKKGG FSIFWADDGL DTGDLLLQKE CEVLPDDTVS TLYNRFLFPE
GIKGMVQAVR LIAEGKAPRL PQPEEGATYE GIQKKETAKI NWDQPAEAIH NWIRGNDKVP
GAWTEACEQK LTFFNSTLST SGLVPEGDTL PIPGAHRPGV VTKAGLILFG NDDRMLLVKN
IQLEDGKMIP ASNFFKGEGS SALELTEVEL AIAEAVRSAW QRILPNVLEV EDSTDFFKSG
AASVDVVRLV EEVKELCDGL ELENEDVYMA STFGDFIQLL VRKLRGDDEE GEYSIDYVEM
AVNKRTLHMP HQLFIGGAFI DAEGAKTFET INPTDGSVIC QVSLPQVTDV DKAVAAAKDA
FENGLWGKIS ARDRGRLLYR LADLMEQHQE ELATIEALDA GAVYTLALKT HVGMSIQTFR
YFAGWCDKIQ GSTIPINQAR PNRNLTLTRK EPVGVCGIII PWNYPLMMLS WKTAACLAAG
NTVVIKPAQV TPLTALKFAE LTLKAGIPKG VVNVLPGSGS LVGQRLSDHP DVRKIGFTGS
TEVGKHIMKS CAVSNVKKVS LELGGKSPLI IFADCDLNKA VQMGMSSVFF NKGENCIAAG
RLFVEDSIHD EFVRRVVEEV RKMKVGNPLD RDTDHGPQNH HAHLMKLIEY CQRGVKEGAT
LICGGKQVPR PGFFFEPTVF TDVEDHMFIA KEESFGPVMI ISRFTDGDID AVLSRANATE
FGLASGVFTR DINKALYVSD KLQAGTVFVN TYNKTDVAAP FGGFKQSGFG KDLGEAALNE
YLRVKTVTFE Y
//
