ID A0A9J7L8Q8_BRAFL Unreviewed; 936 AA.
AC A0A9J7L8Q8;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
DE RecName: Full=formyltetrahydrofolate dehydrogenase {ECO:0000256|ARBA:ARBA00012858};
DE EC=1.5.1.6 {ECO:0000256|ARBA:ARBA00012858};
GN Name=LOC118416886 {ECO:0000313|RefSeq:XP_035678056.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554, ECO:0000313|RefSeq:XP_035678056.1};
RN [1] {ECO:0000313|Proteomes:UP000001554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|Proteomes:UP000001554};
RX PubMed=32313176;
RA Simakov O., Marletaz F., Yue J.X., O'Connell B., Jenkins J., Brandt A.,
RA Calef R., Tung C.H., Huang T.K., Schmutz J., Satoh N., Yu J.K.,
RA Putnam N.H., Green R.E., Rokhsar D.S.;
RT "Deeply conserved synteny resolves early events in vertebrate evolution.";
RL Nat. Ecol. Evol. 0:0-0(2020).
RN [2] {ECO:0000313|RefSeq:XP_035678056.1}
RP IDENTIFICATION.
RC STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035678056.1};
RC TISSUE=Testes {ECO:0000313|RefSeq:XP_035678056.1};
RG RefSeq;
RL Submitted (MAR-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.
CC {ECO:0000256|ARBA:ARBA00007995}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the GART family.
CC {ECO:0000256|ARBA:ARBA00010978}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_035678056.1; XM_035822163.1.
DR GeneID; 118416886; -.
DR KEGG; bfo:118416886; -.
DR OMA; NEQVFMA; -.
DR OrthoDB; 310895at2759; -.
DR Proteomes; UP000001554; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro.
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; 3.40.605.10:FF:000050; Aldehyde dehydrogenase, mitochondrial; 1.
DR FunFam; 3.40.605.10:FF:000026; Aldehyde dehydrogenase, putative; 1.
DR FunFam; 3.40.309.10:FF:000008; 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; 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 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.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR036489-3};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001554}.
FT DOMAIN 351..427
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT ACT_SITE 138
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 705
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 705
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 739
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT BINDING 120..122
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 174
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 629..632
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 662..667
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 682..683
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 836..838
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT SITE 174
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-4"
SQ SEQUENCE 936 AA; 102870 MW; 5245ED3DCB3A84D7 CRC64;
MFFPIAFVAA RQLARPLFVR GFSTSQVYAA NKMKIAVIGQ SQFGTEVYNL LKKEGHEIVG
VFTIPDLQGK PDPLAVAGEK DGVPTFKFPR WRVKGQSIPE VVQQYQACGA DLNVLPFCSQ
XIPMDVINTP KHGSIIYHPS ILPRHRGASA INWTLIHGDK KAGFTIFWAD DGLDTGPILL
QKECYAGPNE TLDGLYNKFL YPEGIKAMAE AVQLIADGKA PRIPQSEDGA TYEPMLKKKE
SVQINWDQTG EALHNFIRGN DKLPGAWTTI NGEQVTLYGS KMFKKEVPEG TEVEVPGASK
PAIVHKGGMI FTGNDGKMLN VKNLQFADGS MIPAKMFGKA DAGGATLELT AEEKDLEGQL
KDVWKGILSI AEIQGETDFF KAGAGSMDVV RLVEEVLQRC SDVSLQNEDV YMNTTFHDFM
QMVVRKARGL DEPDEFEYDA IEMHVNNLKL EFPNQLFINN EFVDASNGAT FDTINPTDES
VICKVSKGTK DDVNTAVKAA KEAFEDGPWG KMNPRDRGKL MYRLADLMDE HKEELATLEA
IDSGAVYTLA LKTHVGMSID TFRYYAGWCD KIMGTTIPIN QARPNHNLTY TKREPVGVVG
LIVPWNYPLM MLAWKMGAAL TPGNTIVLKP AQVTPLTALK FAELAVKAGF PPGVINILPG
AGSQVGQAIL DHPDVRKVGF TGSTPVGKDI MRSCAVSNLK RVSLELGGKS PLVIFNDCDL
DRAVRQSLSG CFFNKGENCI ASGRLFVEES IHDEFVTRVV EEIKKMKIGD PLDRSVDHGP
QNHLAHFNSL LEYCKVGVEQ GAKLVYGGTR VDRPGLFLHP TVFTDVTDDM WIAEEESFGP
VMIISKFKDG DIDGMLKSAN NTEFGLASGV FTKDINKALY VADNLQAGTV FVNTYNKTDV
AAPFGGFKQS GFGKDLGQEA LHEYTRTKAV TVEYWL
//
