ID A0A0P9IQN9_RHOGW Unreviewed; 364 AA.
AC A0A0P9IQN9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=RHOBADRAFT_30660 {ECO:0000313|EMBL:KPV71747.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV71747.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV71747.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV71747.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
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; KQ474091; KPV71747.1; -; Genomic_DNA.
DR RefSeq; XP_018267796.1; XM_018412916.1.
DR AlphaFoldDB; A0A0P9IQN9; -.
DR STRING; 578459.A0A0P9IQN9; -.
DR GeneID; 28973365; -.
DR OMA; HPETEHM; -.
DR OrthoDB; 946665at2759; -.
DR Proteomes; UP000053890; 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}; Reference proteome {ECO:0000313|Proteomes:UP000053890}.
FT DOMAIN 32..126
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 127..312
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 173..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 229..233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 311..314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 356
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 257
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 311
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
SQ SEQUENCE 364 AA; 39533 MW; BE45FE1FFE02EA80 CRC64;
MVKVLAILYD GGKHAEEQPK LLGTTENALG MRPYCEKNGI ELVVTSDKEG PDSEFNKHIV
DADVLITTPF HPGYLTRELI ATAKNLKLAI TAGVGSDHVD LNAANERKIT VAEVTGSNVV
SVAEHVIMTI LVLVRNFVPA HEQIKAGDWE VAAVAKGEYD LEGKVVGTLG AGRIGFRVLQ
RLKPFDCKEL LYYDYNSLPE DAAKEVGVRR VEDLKDFLSQ CDVVTLNCPL HEGTKGIINK
ETISYMKDGA WLVNTARGAL CVAEDVAEAV NSGKLSGYGG DVWPKQPAPA DHCWRTMANP
LTKGGNAMVP HMSGTSLDAQ IRYANGAIKI LDNWRNGVPQ TQSDLITENG EYATLSYGQR
TGKK
//
