ID A0A0B1TI87_OESDE Unreviewed; 846 AA.
AC A0A0B1TI87;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 18-JUN-2025, entry version 46.
DE RecName: Full=10-formyltetrahydrofolate dehydrogenase {ECO:0000256|PIRNR:PIRNR036489};
DE EC=1.5.1.6 {ECO:0000256|PIRNR:PIRNR036489};
GN ORFNames=OESDEN_04234 {ECO:0000313|EMBL:KHJ95811.1};
OS Oesophagostomum dentatum (Nodular worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Oesophagostomum.
OX NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ95811.1, ECO:0000313|Proteomes:UP000053660};
RN [1] {ECO:0000313|EMBL:KHJ95811.1, ECO:0000313|Proteomes:UP000053660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ95811.1,
RC ECO:0000313|Proteomes:UP000053660};
RA Mitreva M.;
RT "Draft genome of the hookworm Oesophagostomum dentatum.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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: 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; KN549840; KHJ95811.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1TI87; -.
DR OrthoDB; 5800189at2759; -.
DR Proteomes; UP000053660; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 FunFam; 1.10.1200.10:FF:000002; 10-formyltetrahydrofolate dehydrogenase; 2.
DR FunFam; 3.40.50.170:FF:000018; 10-formyltetrahydrofolate dehydrogenase; 1.
DR FunFam; 3.40.605.10:FF:000001; Aldehyde dehydrogenase 1; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 2.
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; 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 Pfam; PF00171; Aldedh; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR PIRSF; PIRSF036489; 10-FTHFDH; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53720; ALDH-like; 2.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR PROSITE; PS50075; CARRIER; 2.
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|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036489};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053660};
KW Transferase {ECO:0000313|EMBL:KHJ95811.1}.
FT DOMAIN 327..401
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 507..581
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT BINDING 93..95
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 147
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 815..820
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 835..836
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT SITE 147
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-4"
SQ SEQUENCE 846 AA; 93073 MW; 0177BBA7CC8E8BB2 CRC64;
MKIAIIGQSA FGVDVYKALK KNGHEIVVVF TIPDKNGRED LLAMEAAKDG VPVQKPARWR
KKVADGKFEV LPDMLKLYLS YKAELNVLPF CTQFIPIEVI EAPKYKSIIY HPSILPKHRG
ASAINWTLID GDEEAGLSIF WADDGLDTGP ILLQKKCKVE ENDTLNSLYK RFLYPAGVEA
MAEAVELIAA GKAPRIVQPT EGASYEPYIT AKPELAEIDW SKNQRQLHNF IRGNDKVPGA
WATMNGEKVS VFGSSLYKGK VPPPGAREVE VVGVPGGKVY AHEAGLLLPG SDGKWVNVDT
VKVGSKTIPA HKYGLVEEQG EKLVFTPEEE KIVEEVKKIW AAILKMDVED ETDFFESGGT
SADVTRLVEE IKFHTKVELE NTDIYMGPKF GENAEAVIKK MRGGDKITVE YDPIVMNVNG
MELKFPHELF IDGKFQPSSS GRLYDTINPN DESVICKVPK ADINDVNKAV AAAKAVNVDT
VKVGSKTIPA HKYGLVEEQG EKLVFTPEEE KIVEEVKKIW AAILKMEVED ETDFFESGGT
SADVTRLVEE IKFHTKVELE NTDIYMGPKF GENAEAVIKK MRGGDKITVE YDPIVMNVNG
MELKFPHELF IDGKFQPSSS GRLYDTINPN DESVICKVPK ADINDVNKAV AAAKAAFETG
EWRKMSARER GKRLYKLADL MEEHKEELAT LESLDSGAVY TLALKTHVGM SIDVWRYMAG
WCDKIEGSTI PISNARPNFN LTVTKREPVG VVGLITPWNY PLMMLSWKMS ACLAAGNTVV
HKPAAVTPLT ALKFAELAAL AGIPNGVVNI ITGSGSEIGQ ALADHPDVRK IGFTGSTEVG
AQVMAR
//
