ID G1PEG3_MYOLU Unreviewed; 895 AA.
AC G1PEG3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 78.
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:ENSMLUP00000008906.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000008906.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000008906.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000008906.2}
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; AAPE02044748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02044749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PEG3; -.
DR STRING; 59463.ENSMLUP00000008906; -.
DR Ensembl; ENSMLUT00000009766.2; ENSMLUP00000008906.2; ENSMLUG00000009750.2.
DR eggNOG; KOG2452; Eukaryota.
DR GeneTree; ENSGT00940000160913; -.
DR HOGENOM; CLU_014974_0_0_1; -.
DR InParanoid; G1PEG3; -.
DR OMA; FENGVWG; -.
DR TreeFam; TF354242; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
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:0006740; P:NADPH regeneration; IEA:Ensembl.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
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; 2.
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:UP000001074}.
FT DOMAIN 318..395
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 564..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 666
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 666
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 700
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 623..628
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 643..644
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 750
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 797..799
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 895 AA; 98420 MW; 148F688A67ACB1AA CRC64;
MKIAVIGQSL FGQEVYCHLR KEGYEVVGVF TVPDKNGKAD PLGLEAEKDG VPVFKFPRWR
EKGQALPDVV AKYQALGAEL NVLPFCSQFI PMEVINAPRH GSIIYHPSLL PRHRGASAIN
WTLIHGDKKG GFTVFWADDG LDTGDLLLQR ECEILPDDTV STLYNRFLFP EGIKGMVQAV
RLIAEGRAPR VPQPEEGATY EGIQKKETAK INWEQPAEAI HNWIRGNDKV PGAWTEACGQ
KLTFFNSTLN TAGLVPEGEA LPIPGAHRPG VVTKAGLILF GNDDRMLLVK NIQLEDGKMI
PASHFFRGED SSALELTEAE LVTMEGVRSA WKRILPNVLE VEDSTDFFKS GAASVDVVRL
VEEVKELCDG VELENEDVYM ATTFKDFIQL LVRKLRGDDK ESECIIDYVE KAVNKLTLRM
PHQLFIGGTF VDAEGAKTYE TINPTDGSVI CQVSLAQVSD VDKAVAAAKD AFENGLWGKI
SARDRGRLLY RLADLMEQHQ EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI
QGSTIPINQA RPNRNLTLTR KEPIGVESGH TPEPQEPSVL SRQNMAQSSG LGVDVRVKGL
MPLHPSTSET TLTPLPRLLP SAGSLVGQRL SDHPDVRKIG FTGSTEVGKH IMKSCALSNV
KKVSLELGGK SPLIIFADCD LSKAVQMGMS SVFFNKGENC IAAGRLFVED SIHDQFVQKV
VEEVKKMKIG NPLDRDTNHG PQNHQAHLRK LIEYCQRGVK EGATLVCGGN QVPRPGFFFE
PTVFTDVEDH MFIAKEESFG PVMVISRFAD GDMDTVLSRA NATEFGLASG VFTRDIGKAL
YVSDKLEAGT VFINTYNKTD VAAPFGGFKQ SGFGKDLGEA ALNEYLRVKT VTFEY
//
