位置:首页 > 蛋白库 > FDH_CHATD
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024