ID A0A3B3DQ58_ORYME Unreviewed; 1006 AA.
AC A0A3B3DQ58;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=formyltetrahydrofolate dehydrogenase {ECO:0000256|ARBA:ARBA00012858};
DE EC=1.5.1.6 {ECO:0000256|ARBA:ARBA00012858};
GN Name=ALDH1L2 {ECO:0000313|Ensembl:ENSOMEP00000031490.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000031490.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000031490.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- 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}.
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DR AlphaFoldDB; A0A3B3DQ58; -.
DR STRING; 30732.ENSOMEP00000031490; -.
DR PaxDb; 30732-ENSOMEP00000031490; -.
DR Ensembl; ENSOMET00000022817.1; ENSOMEP00000031490.1; ENSOMEG00000016356.1.
DR GeneTree; ENSGT00940000158018; -.
DR OMA; NEQVFMA; -.
DR Proteomes; UP000261560; Unplaced.
DR GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IEA:UniProtKB-EC.
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:UniProt.
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; 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:SF131; MITOCHONDRIAL 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 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 422..499
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 30..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 777
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 1006 AA; 110680 MW; F92E58FAF27A5614 CRC64;
MIKAVDNLMQ NTPAFYLKGT GGYVDDRSPP FHPPPPSCRV SGLAGASREG MTEPGGNCHV
SLRTRQKHAH MCRKPDTLAH APLGRRLRGR EEDINRTAIR YYQKKLKLAI IGQSVFGQEV
YSSLRKQGHK VVGVFTVPDK DGKADPLAVA AEKDGTPLFK FPRWRNKGQP LPEVVEAYKS
VGAELNVMPF CSQFIPMTVI DHPQHGSIIY HPSILPLHRG ASAINWTLIH GDQKAGFTVF
WADDGLDTGP ILLQRECAVE PDDTVDTLYN RFLFPEGIKA MVESVQLIAD GKAPRIPQPE
EGASYEGIQR KSNAKVDLAQ PAKAIHNWIR GHDKVPGAWA HIGGQSVTFY GSSMLSEPVP
AGQPLEIEGA SQPGIISKKG LVLFGTDGKA LLVKNLQFED GKMIPASKYF SSGESSSVEL
TDEEKKMAEE IRNIWKGILS NVPAIVDTTD FFKSGAASMD VVRLVEEVKQ KCVGVQLQNE
DVYMATTFQD FIQMFVRKLR GEDQEEELVV DYATKEVNSM TVKMPYQCFI NGRFENAEDG
KTYNTINPTD GSVICKVSYA AVSDVDRAVA AAKEAFDNGP WGRMNPRDRG SLLYKLADLM
EEHQEELATI ESIDSGAVYT LALKTHVGMS IQTFRYFAGW CDKIQGKTIP INQARPNRNL
TFTKKEPLGV CAIVIPWNYP LMMLAWKSAA CLAAGNTLVL KPAQVTPLTA LKFAELSVKA
GIPKGVINIL PGSGGMVGQR LSDHPDIRKL GFTGSTPIGK QIMKSCALSN LKKVSLELGG
KSPLIIFSDC DMDKAVRMGM SSVFFNKGEN CIAAGRLFVE ESIHDEYIRR VVEEIMKMKI
GDPLDRSTDH GPQNHKAHLD KLLEYCDIGV KEGATLVYGG KQVDRPGFFM QPTVFTDVED
HMFIAKEESF GPVMVVSKFK DGDVDGVLQR ANDTEYGLAS GVFTRDINKA MYVSERLEAG
TVFVNTYNKT DVASPFGGFK QSGFGKDLGE DALSEYLKTK AVTVEY
//
