ID A0A2J8KAV5_PANTR Unreviewed; 902 AA.
AC A0A2J8KAV5; A0A2I3T7D1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:ENSPTRP00000085149.1,
GN ECO:0000313|VGNC:VGNC:57672};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000085149.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000085149.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000085149.1}
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 EMBL; AACZ04048130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_016797323.1; XM_016941834.1.
DR RefSeq; XP_016797324.1; XM_016941835.1.
DR RefSeq; XP_016797325.1; XM_016941836.1.
DR AlphaFoldDB; A0A2J8KAV5; -.
DR STRING; 9598.ENSPTRP00000085149; -.
DR Ensembl; ENSPTRT00000087455.1; ENSPTRP00000085149.1; ENSPTRG00000043503.1.
DR GeneID; 460655; -.
DR KEGG; ptr:460655; -.
DR CTD; 10840; -.
DR VGNC; VGNC:57672; ALDH1L1.
DR GeneTree; ENSGT00940000160913; -.
DR InParanoid; A0A2J8KAV5; -.
DR OrthoDB; 2291791at2759; -.
DR Proteomes; UP000002277; Chromosome 3.
DR Bgee; ENSPTRG00000043503; Expressed in liver and 16 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:UniProtKB-UniRule.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006740; P:NADPH regeneration; IEA:Ensembl.
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:UP000002277}.
FT DOMAIN 318..395
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 673
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 673
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 707
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 571..573
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 597..600
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 630..635
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 650..651
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 757
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 804..806
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 902 AA; 98767 MW; 5D0D2209F6503DA1 CRC64;
MKIAVIGQSL FGQEVYCHLR KEGHEVVGVF TVPDKDGKAD PLGLEAEKDG VPVFKFSRWR
AKGQALPDVV AKYQALGAEL NVLPFCSQFI PMEIISAPRH GSIIYHPSLL PRHRGASAIN
WTLIHGDKKG GFSIFWADDG LDTGDLLLQK ECEVLPDDTV STLYNRFLFP EGIKGMVQAV
RLISEGKAPR LPQPEEGATY EGIQKKETAK INWDQPAEAI HNWIRGNDKV PGAWTEACEQ
KLTFFNSTLN TSGLVPEGDA LPIPGAHRPG VVTKAGLILF GNDDKMLLVK NIQLEDGKMI
LASNFFKGAA SSVLELTEAE LVTAEAVRSV WQRILPNVLE VEDSTDFFKS GAASVDVVRL
VEEVKELCDG LELENEDVYM ASTFGDFIQL LVRKLRGDDE EGECSIDYVE MAVNKRTVRM
PHQLFIGGEF VDAEGAKTSE TINPTDGSVI CQVSLAQVTD VDKAVAAAKD AFENGRWGKI
SARDRGRLMY RLADLMEQHQ EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI
QGSTIPINQA RPNRNLTLTR KEPVGVCGII IPWNYPLMML SWKTAACLAA GNTVVIKPAQ
VTPLTALKFA ELTLKAGIPK GVVNVLPGSG SLVGQRLSDH PDVRKIGFTG STEVGKHIMK
SCAISNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF FNKGENCIAA GRLFVEDSIH
DEFVRRVVEE VRKMKVGNPL DRDTDHGPQN HHAHLVKLME YCQCGVKEGA TLVCGGNQVP
RPGFFFEPTV FTDVEDHMFI AKEESFGPVM IISRFADGDV DAVLSRANAT EFGLASGVFT
RDINKALYVS DKLQAGTVFV NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRVKTVTF
EY
//