FDH_CHATD
ID FDH_CHATD Reviewed; 370 AA.
AC G0SGU4;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000305};
DE Short=FDH {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000303|Ref.2};
DE EC=1.17.1.9 {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|Ref.2};
DE AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000303|Ref.2};
GN Name=FDH {ECO:0000303|Ref.2}; ORFNames=CTHT_0067590;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.1016/j.molcatb.2015.09.014;
RA Ozgun G., Karaguler N.G., Turunen O., Turner N.J., Binay B.;
RT "Characterization of a new acidic NAD(+)-dependent formate dehydrogenase
RT from thermophilic fungus Chaetomium thermophilum.";
RL J. Mol. Catal., B Enzym. 122:212-217(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:0000255|HAMAP-Rule:MF_03210, ECO:0000269|Ref.2}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03210, ECO:0000269|Ref.2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.2 mM for formate (at pH 5.0 and 25 degrees Celsius)
CC {ECO:0000269|Ref.2};
CC KM=1.8 mM for NAD (at pH 5.0 and 25 degrees Celsius)
CC {ECO:0000269|Ref.2};
CC Note=kcat is 0.8 sec(-1) with formate as substrate.
CC {ECO:0000269|Ref.2};
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Thermostable up to 55 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03210}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. FDH subfamily. {ECO:0000255|HAMAP-Rule:MF_03210}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL988047; EGS17433.1; -; Genomic_DNA.
DR RefSeq; XP_006697051.1; XM_006696988.1.
DR PDB; 6T8Y; X-ray; 1.26 A; AAA/BBB/CCC/DDD=1-370.
DR PDB; 6T8Z; X-ray; 1.21 A; AAA/BBB/CCC/DDD=1-370.
DR PDB; 6T92; X-ray; 1.12 A; AAA/BBB/CCC/DDD=1-370.
DR PDB; 6T94; X-ray; 1.15 A; AAA/BBB/CCC/DDD=1-370.
DR PDBsum; 6T8Y; -.
DR PDBsum; 6T8Z; -.
DR PDBsum; 6T92; -.
DR PDBsum; 6T94; -.
DR AlphaFoldDB; G0SGU4; -.
DR SMR; G0SGU4; -.
DR STRING; 759272.G0SGU4; -.
DR PRIDE; G0SGU4; -.
DR EnsemblFungi; EGS17433; EGS17433; CTHT_0067590.
DR GeneID; 18260797; -.
DR KEGG; cthr:CTHT_0067590; -.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_0_0_1; -.
DR OrthoDB; 700058at2759; -.
DR BRENDA; 1.17.1.9; 1279.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009326; C:formate dehydrogenase complex; IEA:UniProtKB-EC.
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 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 Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..370
FT /note="Formate dehydrogenase"
FT /id="PRO_0000435287"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 175..176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 231..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 257
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 312..315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT SITE 259
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT SITE 312
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
SQ SEQUENCE 370 AA; 40845 MW; 05DA977DA8165BB8 CRC64;
MVKVLAVLYD GGEHAKQVPG LLGTTENELG LRKWLEDQGH TLVTTSDKDR EGSTFDRELE
DAEIIITTPF HPGYLTAERL ARAKKLKLAV TAGIGSDHVD LDAANKTNGG ITVAEVTGSN
VVSVAEHVVM TILVLVRNFV PAHEQIEAGR WDVAEVAKDE YDLEGKVVGT VGVGRIGERV
LRRLKGFDCK ELLYYDYQPL SPEKEKEIGC RRVENLEEML AQCDVVTINC PLHESTRGLF
NKDLISKMKR GSWLVNTARG AIVVKEDVAE ALRTGHLRGY GGDVWFPQPA PADHVLRTAK
NPFGGGNAMV PHMSGTSLDA QKRYAEGVKR ILDSYLSGRF DYRPEDLIVH QGKYATRAYG
QREDVKIPGQ