ID W1P9Q2_AMBTC Unreviewed; 380 AA.
AC W1P9Q2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Formate dehydrogenase, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03210};
DE Short=FDH {ECO:0000256|HAMAP-Rule:MF_03210};
DE EC=1.17.1.9 {ECO:0000256|HAMAP-Rule:MF_03210};
DE AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03210};
GN ORFNames=AMTR_s00058p00174910 {ECO:0000313|EMBL:ERN06637.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN06637.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to carbon
CC dioxide. Involved in the cell stress response. {ECO:0000256|HAMAP-
CC Rule:MF_03210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000455, ECO:0000256|HAMAP-
CC Rule:MF_03210};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03210}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03210}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. FDH subfamily. {ECO:0000256|HAMAP-Rule:MF_03210}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03210}.
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DR EMBL; KI393888; ERN06637.1; -; Genomic_DNA.
DR RefSeq; XP_006844962.1; XM_006844899.2.
DR AlphaFoldDB; W1P9Q2; -.
DR STRING; 13333.W1P9Q2; -.
DR EnsemblPlants; ERN06637; ERN06637; AMTR_s00058p00174910.
DR GeneID; 18434836; -.
DR Gramene; ERN06637; ERN06637; AMTR_s00058p00174910.
DR KEGG; atr:18434836; -.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_0_0_1; -.
DR OMA; EFDMEDK; -.
DR OrthoDB; 946665at2759; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0042183; P:formate catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd05302; FDH; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR HAMAP; MF_03210; Formate_dehydrogenase; 1.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR033689; FDH_NAD-dep.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03210};
KW NAD {ECO:0000256|HAMAP-Rule:MF_03210};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03210}; Reference proteome {ECO:0000313|Proteomes:UP000017836}.
FT DOMAIN 67..360
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 158..336
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 203..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 258..262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 310
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 334..337
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 286
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 334
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
SQ SEQUENCE 380 AA; 41608 MW; A3210064EF7EE79A CRC64;
MAISRAAASV IPALLSKGPA ISRHLHASSG SKKIVGVFYK ANEYASMNPN FLGCAENALG
IKGWLESQGH QYIVTDDKEG PYCELEKHIP DLHVLISTPF HPAYVTAERI KKAKNLELLL
TAGIGSDHID LKAAAAAGLT VAEITGSNVV SVAEDELMRI LILVRNFLPG YHQVIKGEWN
VAAIAYRAYD LEGKTIGTVG AGRIGKLLLQ RLKPFNCNLL YHDRIKMEHE LEAQIGAQFE
PDVDAMLPKC DVIVINTPLT EKTKGMFDKN RIAKLKKGVL IVNNARGAIM DTDAVAEACS
NGHIGGYSGD VWNPQPAPKD HPWRYMPNHA MTPHISGTTI DGQIRYAAGV KDMLERYFKG
EDFPPQNYIV KEGKLASQYV
//
