ID A0A2G5U4M3_9PELO Unreviewed; 908 AA.
AC A0A2G5U4M3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=10-formyltetrahydrofolate dehydrogenase {ECO:0000256|PIRNR:PIRNR036489};
DE EC=1.5.1.6 {ECO:0000256|PIRNR:PIRNR036489};
GN Name=Cni-alh-3 {ECO:0000313|EMBL:PIC34186.1};
GN Synonyms=Cnig_chr_IV.g13916 {ECO:0000313|EMBL:PIC34186.1};
GN ORFNames=B9Z55_013916 {ECO:0000313|EMBL:PIC34186.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC34186.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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. {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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIC34186.1}.
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DR EMBL; PDUG01000004; PIC34186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5U4M3; -.
DR STRING; 1611254.A0A2G5U4M3; -.
DR Proteomes; UP000230233; Chromosome iv.
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:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08703; FDH_Hydrolase_C; 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:SF190; 10-FORMYLTETRAHYDROFOLATE DEHYDROGENASE; 1.
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.
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|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:UP000230233}.
FT DOMAIN 328..402
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 679
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 679
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 713
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT BINDING 94..96
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 148
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 603..606
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 656..657
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 763
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 810..812
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT SITE 148
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-4"
SQ SEQUENCE 908 AA; 99276 MW; 054CF703028834C0 CRC64;
MKIAIIGQSA FGVDVYKELR KNGHEIVVVF TIPDKNGRED LLAVEAAKDG VPVQKPARWR
KKNPETGKFE TLPEMLELYK SFGAELNVLP FCTQFIPLEI TEAPPKKSII YHPSILPKHR
GASAINWTLI EGDEEAGLSI FWADDGLDTG PILLQKKCKV EENDTLNTLY KRFLYPAGVA
AVAESVELIA SGKAPRIVQP EEGASYEPYI TTKPELAQID WSKTQRQLHN FIRGNDKVPG
AWAILNGEKV SFFGSKLWKP KKLPEDAVEV AVAEVPGGKV LVEDRGLLLP GSDGKWVIVD
TVKIGTKTIP ASKYGQGADQ VEELVLTDDE KNVMAKLKKI WAGILKTQVS SDTDFFESGA
SSADVTRLVE EIKFNTGAEL ESGHIYSGPT LGENIDIVVR NLRGEGGLSV TYDPIVLNVN
NMELKFPHEQ FIDGKFVGSS DGRTFQTINP ATEKPICSLP LATVADVDRA VRAAKKAFER
GEWRQMSARE RGKRLYRLAE LMEEHKEELA TLESLDAGAV YTLALKTHVG MSIDVWRYFA
GWCDKIQGKT IPISNARPNK NLCLTVREPI GVVGLITPWN YPLMMLSWKM AACLAAGNTV
VHKPAQVTPL TALKFAELSV LAGIPPGVIN IVTGSGSLVG NRLTAHPDVR KIGFTGSTEI
GATVMESCAK SNIKKVSLEL GGKSPLIIFA DADLEKAVKQ ACGAVFFNKG ENCIAAGRVF
IAKSIHDSFV KKLVEEAKQY QIGDPLDRST AHGPQNHLAH LNKLVEYVEN AVRDGAKVEV
GGKRLEREGL FFPPTILSNI DDENFAASEE SFGPIMCISS FDDDDVEDVL RRANDTEFGL
AAGVFTRDAS KSLRVAEALH AGTVFVNTYQ KTDVAAPFGG FKQSGFGKDM GEEALNEYLV
TKTITIEY
//
