ID A0A8C4HCV5_DICLA Unreviewed; 889 AA.
AC A0A8C4HCV5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 2.
DT 28-JAN-2026, entry version 20.
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:ENSDLAP00005040258.2};
OS Dicentrarchus labrax (European seabass) (Morone labrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Moronidae; Dicentrarchus.
OX NCBI_TaxID=13489 {ECO:0000313|Ensembl:ENSDLAP00005040258.2, ECO:0000313|Proteomes:UP000694389};
RN [1] {ECO:0000313|Ensembl:ENSDLAP00005040258.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDLAP00005040258.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-10-formyltetrahydrofolate + NADP(+) + H2O = (6S)-5,6,7,8-
CC tetrahydrofolate + CO2 + NADPH + H(+); 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:ARBA00048239};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10181;
CC Evidence={ECO:0000256|ARBA:ARBA00048239};
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; A0A8C4HCV5; -.
DR Ensembl; ENSDLAT00005042975.2; ENSDLAP00005040258.2; ENSDLAG00005017771.2.
DR GeneTree; ENSGT00940000160913; -.
DR Proteomes; UP000694389; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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: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 FunFam; 1.10.1200.10:FF:000002; 10-formyltetrahydrofolate dehydrogenase; 1.
DR FunFam; 3.10.25.10:FF:000002; 10-formyltetrahydrofolate dehydrogenase; 1.
DR FunFam; 3.40.50.170:FF:000002; 10-formyltetrahydrofolate dehydrogenase; 1.
DR FunFam; 3.40.309.10:FF:000008; Cytosolic 10-formyltetrahydrofolate dehydrogenase; 1.
DR FunFam; 3.40.605.10:FF:000009; Cytosolic 10-formyltetrahydrofolate dehydrogenase; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1.
DR Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 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 Pfam; PF00171; Aldedh; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR PIRSF; PIRSF036489; 10-FTHFDH; 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 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|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036489};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694389}.
FT DOMAIN 307..384
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 662
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 662
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 696
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT BINDING 88..90
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 142
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 560..562
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 586..589
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 619..624
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 639..640
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 746
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 793..795
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT SITE 142
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-4"
SQ SEQUENCE 889 AA; 97611 MW; DD2F7A6749561E39 CRC64;
MKIAVIGQSL FGQEVYKELR KDGHTIVGVF TIPDKDGKAD PLATEAEKDG VPVFKFPRWR
VKGQAIPEVV AQYKATGAEL NVLPFCSQFI PMEVIDHPKH GSIIYHPSLL PRHRGASAIN
WTLIHGDRKG GFTVFWADDG LDTGPILLQR ECDVDPNDTV NTIYKRFLFP EGVKGTVEAV
RLIAEGKAPR ITQPQEGATY ECIQKKDNSK SAEALHNWIR GNDKVPGAWA EVDGQKVTFY
GSSLVDNSPT NGQPLEIPGA SQPGIVTKAG LVLFGNDSKA LLVKNLQFED GKMIAAAQYF
NSGSSAAVEL TEEEKTFAVW QSILTNVTEI EDSTDFFKSG AASMDVVRLV EEVKLRASGC
QLQNEDVYMN TTFQDFIQMC VRKLRGEDGE EELVVDYVSK NINNMTIKMP HQLFINGEFV
DADGGKTYKT INPTDGTAIC DVSLAQISDV DRAVAAAKEA FEEGEWGRMN PRDRGRLIYR
LADLMEEHQE ELATIEAIDS GAVYTLALKT HVGMSIQTFR YFAGWCDKIQ GSTIPINQAR
PNRNLTFTKK EPIGVCAIVI PWNYPLMMLA WKTAACLAAG NTVVLKPAQV TPLTALKFAE
LAARAGLPKG VVNILPGSGA LVGQRLSDHP DVRKLGFTGS TEIGKHIMKS CAVSNVKKVS
LELGGKSPLI IFGDCDMDKA VRMGMSSVFF NKGENCIAAG RLFVEDTIHD QFVKRVVEEV
KKMKIGDPLD RSTDHGPQNH KAHLDKLVEY CQTGIKEGAT LVCGSKQVQR PGFFFEPTLF
TDVQDHMYIA KEESFGPVMI ISKFKSGDVD DVLRRANATE YGLASGVFTR DISKALYVSE
KLNAGTVFVN TYNKTDVASP FGGFKQSGFG KDLGEKNLEH TPADKINLK
//
