ID A0A3N4LR09_9PEZI Unreviewed; 372 AA.
AC A0A3N4LR09;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128, ECO:0000256|HAMAP-Rule:MF_03210};
DE Short=FDH {ECO:0000256|HAMAP-Rule:MF_03210};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128, ECO:0000256|HAMAP-Rule:MF_03210};
DE AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03210};
GN ORFNames=L211DRAFT_836699 {ECO:0000313|EMBL:RPB25367.1};
OS Terfezia boudieri ATCC MYA-4762.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pezizaceae; Terfezia.
OX NCBI_TaxID=1051890 {ECO:0000313|EMBL:RPB25367.1, ECO:0000313|Proteomes:UP000267821};
RN [1] {ECO:0000313|EMBL:RPB25367.1, ECO:0000313|Proteomes:UP000267821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4762 {ECO:0000313|EMBL:RPB25367.1,
RC ECO:0000313|Proteomes:UP000267821};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to carbon
CC dioxide. Formate oxidation is the final step in the methanol oxidation
CC pathway in methylotrophic microorganisms. Has a role in the
CC detoxification of exogenous formate in non-methylotrophic organisms.
CC {ECO:0000256|HAMAP-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: Cytoplasm {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; ML121538; RPB25367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4LR09; -.
DR STRING; 1051890.A0A3N4LR09; -.
DR InParanoid; A0A3N4LR09; -.
DR Proteomes; UP000267821; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
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 Cytoplasm {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}; Pyruvate {ECO:0000313|EMBL:RPB25367.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000267821}.
FT DOMAIN 44..329
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 134..305
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 179..180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 235..239
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 316..319
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 263
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 316
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
SQ SEQUENCE 372 AA; 40857 MW; 2593573C2DF2B0CC CRC64;
MAQQAKKRKI LAVLYEGREH SQQVPGLLGT VENELGLRKW IEGKGYELVT TADKEGPNSA
FEKELVDAEV IITTPFHPGY LTAERLHKAL KLKLAVTAGV GSDHVDLDVA CQKGITVAEV
TGSNVVSVAE HVVMTILSLV RNFVPAHEQI ARGDWDVAAV AKDSYDLEGK VVGTVGIGRI
GERVLRRLKP FDCKDLLYYD YQPLNPEIEK EIGCRGVKSV EKLVKQCDII TINCPLHHGT
RGLFDKDLLA KMKKGSWLVN TARGAIVVKE DVAEALKSGH LRGYGGDVWF PQPAPKDHPL
RYALNPFGGG NAMVPHMSGT TIDAQKRYAA GTKCILESYF SGKGDYRPQD LIILEGKYAT
HAYGKDSKEN KK
//
