ADHX_HUMAN
ID ADHX_HUMAN Reviewed; 374 AA.
AC P11766; Q6FHR2;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Alcohol dehydrogenase class-3 {ECO:0000305};
DE EC=1.1.1.1 {ECO:0000269|PubMed:8460164};
DE AltName: Full=Alcohol dehydrogenase 5;
DE AltName: Full=Alcohol dehydrogenase class chi chain;
DE AltName: Full=Alcohol dehydrogenase class-III;
DE AltName: Full=Glutathione-dependent formaldehyde dehydrogenase;
DE Short=FALDH;
DE Short=FDH;
DE Short=GSH-FDH;
DE EC=1.1.1.-;
DE AltName: Full=S-(hydroxymethyl)glutathione dehydrogenase;
DE EC=1.1.1.284 {ECO:0000269|PubMed:8460164};
GN Name=ADH5 {ECO:0000312|HGNC:HGNC:253}; Synonyms=ADHX, FDH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2818582; DOI=10.1016/0006-291x(89)91507-6;
RA Sharma C.P., Fox E.A., Holmquist B., Joernvall H., Vallee B.L.;
RT "cDNA sequence of human class III alcohol dehydrogenase.";
RL Biochem. Biophys. Res. Commun. 164:631-637(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2679557; DOI=10.1016/0006-291x(89)91741-5;
RA Giri P.R., Krug J.F., Kozak C., Moretti T., O'Brien S.J., Seuanez H.N.,
RA Goldman D.;
RT "Cloning and comparative mapping of a human class III (chi) alcohol
RT dehydrogenase cDNA.";
RL Biochem. Biophys. Res. Commun. 164:453-460(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1446828; DOI=10.1016/0378-1119(92)90135-c;
RA Hur M.W., Edenberg H.J.;
RT "Cloning and characterization of the ADH5 gene encoding human alcohol
RT dehydrogenase 5, formaldehyde dehydrogenase.";
RL Gene 121:305-311(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-163 AND ILE-309.
RG NIEHS SNPs program;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-374, AND COFACTOR.
RC TISSUE=Liver;
RX PubMed=3365377; DOI=10.1021/bi00404a009;
RA Kaiser R., Holmquist B., Hempel J., Vallee B.L., Joernvall H.;
RT "Class III human liver alcohol dehydrogenase: a novel structural type
RT equidistantly related to the class I and class II enzymes.";
RL Biochemistry 27:1132-1140(1988).
RN [9]
RP PARTIAL PROTEIN SEQUENCE, AND MUTAGENESIS OF ARG-115.
RX PubMed=8494891; DOI=10.1021/bi00070a024;
RA Holmquist B., Moulis J.-M., Engeland K., Vallee B.L.;
RT "Role of arginine 115 in fatty acid activation and formaldehyde
RT dehydrogenase activity of human class III alcohol dehydrogenase.";
RL Biochemistry 32:5139-5144(1993).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-115.
RX PubMed=8460164; DOI=10.1073/pnas.90.6.2491;
RA Engeland K., Hoeoeg J.-O., Holmquist B., Estonius M., Joernvall H.,
RA Vallee B.L.;
RT "Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding
RT site required for formaldehyde dehydrogenase activity and fatty acid
RT activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2491-2494(1993).
RN [11]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16081420; DOI=10.1074/jbc.m504055200;
RA Collins X.H., Harmon S.D., Kaduce T.L., Berst K.B., Fang X., Moore S.A.,
RA Raju T.V., Falck J.R., Weintraub N.L., Duester G., Plapp B.V.,
RA Spector A.A.;
RT "Omega-oxidation of 20-hydroxyeicosatetraenoic acid (20-HETE) in cerebral
RT microvascular smooth muscle and endothelium by alcohol dehydrogenase 4.";
RL J. Biol. Chem. 280:33157-33164(2005).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-351, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND SUBUNIT.
RX PubMed=9018047; DOI=10.1006/jmbi.1996.0731;
RA Yang Z.-N., Bosron W.F., Hurley T.D.;
RT "Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent
RT formaldehyde dehydrogenase.";
RL J. Mol. Biol. 265:330-343(1997).
CC -!- FUNCTION: Catalyzes the oxidation of long-chain primary alcohols and
CC the oxidation of S-(hydroxymethyl) glutathione (PubMed:8460164). Also
CC oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE,
CC producing both the intermediate aldehyde, 20-oxoarachidonate and the
CC end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate
CC (PubMed:16081420). Class-III ADH is remarkably ineffective in oxidizing
CC ethanol (PubMed:8460164). {ECO:0000269|PubMed:16081420,
CC ECO:0000269|PubMed:8460164}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:8460164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:8460164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-
CC formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58758; EC=1.1.1.284;
CC Evidence={ECO:0000269|PubMed:8460164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-
CC formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58758; EC=1.1.1.284;
CC Evidence={ECO:0000269|PubMed:8460164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=20-oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H2O + NAD(+) =
CC (5Z,8Z,11Z,14Z)-eicosatetraenedioate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:39803, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76645,
CC ChEBI:CHEBI:76647; Evidence={ECO:0000269|PubMed:16081420};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39804;
CC Evidence={ECO:0000305|PubMed:16081420};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + NAD(+) = 20-
CC oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + NADH;
CC Xref=Rhea:RHEA:39799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:76624, ChEBI:CHEBI:76645;
CC Evidence={ECO:0000269|PubMed:16081420};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39800;
CC Evidence={ECO:0000305|PubMed:16081420};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:3365377};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:3365377};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for 20-HETE {ECO:0000269|PubMed:16081420};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9018047}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: There are 7 different ADH's isozymes in human: three
CC belongs to class-I: alpha, beta, and gamma, one to class-II: pi, one to
CC class-III: chi, one to class-IV: ADH7 and one to class-V: ADH6.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/adh5/";
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DR EMBL; M30471; AAA79018.1; -; mRNA.
DR EMBL; M29872; AAA51597.1; -; mRNA.
DR EMBL; M81118; AAA51596.1; -; Genomic_DNA.
DR EMBL; M81112; AAA51596.1; JOINED; Genomic_DNA.
DR EMBL; M81113; AAA51596.1; JOINED; Genomic_DNA.
DR EMBL; M81114; AAA51596.1; JOINED; Genomic_DNA.
DR EMBL; M81115; AAA51596.1; JOINED; Genomic_DNA.
DR EMBL; M81116; AAA51596.1; JOINED; Genomic_DNA.
DR EMBL; M81117; AAA51596.1; JOINED; Genomic_DNA.
DR EMBL; CR541689; CAG46490.1; -; mRNA.
DR EMBL; BT019832; AAV38635.1; -; mRNA.
DR EMBL; AY987960; AAX81412.1; -; Genomic_DNA.
DR EMBL; BC014665; AAH14665.1; -; mRNA.
DR CCDS; CCDS47111.1; -.
DR PIR; JH0789; DEHUC2.
DR RefSeq; NP_000662.3; NM_000671.4.
DR PDB; 1M6H; X-ray; 2.00 A; A/B=2-374.
DR PDB; 1M6W; X-ray; 2.30 A; A/B=2-374.
DR PDB; 1MA0; X-ray; 2.30 A; A/B=2-374.
DR PDB; 1MC5; X-ray; 2.60 A; A/B=1-374.
DR PDB; 1MP0; X-ray; 2.20 A; A/B=2-374.
DR PDB; 1TEH; X-ray; 2.70 A; A/B=2-374.
DR PDB; 2FZE; X-ray; 1.90 A; A/B=2-374.
DR PDB; 2FZW; X-ray; 1.84 A; A/B=2-374.
DR PDB; 3QJ5; X-ray; 1.90 A; A/B=2-374.
DR PDBsum; 1M6H; -.
DR PDBsum; 1M6W; -.
DR PDBsum; 1MA0; -.
DR PDBsum; 1MC5; -.
DR PDBsum; 1MP0; -.
DR PDBsum; 1TEH; -.
DR PDBsum; 2FZE; -.
DR PDBsum; 2FZW; -.
DR PDBsum; 3QJ5; -.
DR AlphaFoldDB; P11766; -.
DR SMR; P11766; -.
DR BioGRID; 106640; 30.
DR IntAct; P11766; 10.
DR MINT; P11766; -.
DR STRING; 9606.ENSP00000296412; -.
DR BindingDB; P11766; -.
DR ChEMBL; CHEMBL4116; -.
DR DrugBank; DB03704; 12-Hydroxydodecanoic Acid.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB01020; Isosorbide mononitrate.
DR DrugBank; DB03017; Lauric acid.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB12612; Ozanimod.
DR DrugBank; DB11077; Polyethylene glycol 400.
DR DrugBank; DB04153; S-Hydroxymethyl Glutathione.
DR SwissLipids; SLP:000000500; -.
DR CarbonylDB; P11766; -.
DR GlyGen; P11766; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P11766; -.
DR MetOSite; P11766; -.
DR PhosphoSitePlus; P11766; -.
DR SwissPalm; P11766; -.
DR BioMuta; ADH5; -.
DR DMDM; 113408; -.
DR REPRODUCTION-2DPAGE; IPI00746777; -.
DR EPD; P11766; -.
DR jPOST; P11766; -.
DR MassIVE; P11766; -.
DR PaxDb; P11766; -.
DR PeptideAtlas; P11766; -.
DR PRIDE; P11766; -.
DR ProteomicsDB; 52803; -.
DR Antibodypedia; 25845; 450 antibodies from 37 providers.
DR DNASU; 128; -.
DR Ensembl; ENST00000296412.14; ENSP00000296412.8; ENSG00000197894.12.
DR GeneID; 128; -.
DR KEGG; hsa:128; -.
DR MANE-Select; ENST00000296412.14; ENSP00000296412.8; NM_000671.4; NP_000662.3.
DR CTD; 128; -.
DR DisGeNET; 128; -.
DR GeneCards; ADH5; -.
DR HGNC; HGNC:253; ADH5.
DR HPA; ENSG00000197894; Low tissue specificity.
DR MalaCards; ADH5; -.
DR MIM; 103710; gene.
DR neXtProt; NX_P11766; -.
DR OpenTargets; ENSG00000197894; -.
DR PharmGKB; PA24574; -.
DR VEuPathDB; HostDB:ENSG00000197894; -.
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00940000155196; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; P11766; -.
DR OMA; IHHYMGT; -.
DR OrthoDB; 664798at2759; -.
DR PhylomeDB; P11766; -.
DR TreeFam; TF300429; -.
DR BioCyc; MetaCyc:HS10601-MON; -.
DR PathwayCommons; P11766; -.
DR Reactome; R-HSA-71384; Ethanol oxidation.
DR SABIO-RK; P11766; -.
DR SignaLink; P11766; -.
DR BioGRID-ORCS; 128; 120 hits in 1079 CRISPR screens.
DR ChiTaRS; ADH5; human.
DR EvolutionaryTrace; P11766; -.
DR GeneWiki; ADH5; -.
DR GenomeRNAi; 128; -.
DR Pharos; P11766; Tchem.
DR PRO; PR:P11766; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P11766; protein.
DR Bgee; ENSG00000197894; Expressed in mucosa of stomach and 209 other tissues.
DR ExpressionAtlas; P11766; baseline and differential.
DR Genevisible; P11766; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
DR GO; GO:0018467; F:formaldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR GO; GO:0010430; P:fatty acid omega-oxidation; IDA:UniProtKB.
DR GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central.
DR GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IEA:Ensembl.
DR GO; GO:0045777; P:positive regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0003016; P:respiratory system process; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0051409; P:response to nitrosative stress; IEA:Ensembl.
DR GO; GO:0051775; P:response to redox state; IDA:UniProtKB.
DR GO; GO:0001523; P:retinoid metabolic process; IEA:Ensembl.
DR CDD; cd08300; alcohol_DH_class_III; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR014183; ADH_3.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02818; adh_III_F_hyde; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Lipid metabolism; Metal-binding; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3365377,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..374
FT /note="Alcohol dehydrogenase class-3"
FT /id="PRO_0000160759"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:3365377"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:3365377"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3365377"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3365377"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3365377"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3365377"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:3365377"
FT SITE 115
FT /note="Important for FDH activity and activation by fatty
FT acids"
FT /evidence="ECO:0000269|PubMed:8460164,
FT ECO:0000269|PubMed:8494891"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 233
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28474"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 315
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28474"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 163
FT /note="L -> S (in dbSNP:rs28730623)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025823"
FT VARIANT 309
FT /note="V -> I (in dbSNP:rs28730628)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025824"
FT VARIANT 353
FT /note="D -> E (in dbSNP:rs16996593)"
FT /id="VAR_048199"
FT MUTAGEN 115
FT /note="R->A,D: Loss of FDH activity and loss of activation
FT by fatty acids."
FT /evidence="ECO:0000269|PubMed:8460164,
FT ECO:0000269|PubMed:8494891"
FT CONFLICT 167
FT /note="D -> Y (in Ref. 2; AAA51597)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="F -> L (in Ref. 2; AAA51597)"
FT /evidence="ECO:0000305"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3QJ5"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2FZW"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:2FZW"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 229..235
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:2FZW"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:2FZW"
FT HELIX 355..363
FT /evidence="ECO:0007829|PDB:2FZW"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:2FZW"
SQ SEQUENCE 374 AA; 39724 MW; F4F823B4A609C952 CRC64;
MANEVIKCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKII ATAVCHTDAY TLSGADPEGC
FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC KFCLNPKTNL CQKIRVTQGK
GLMPDGTSRF TCKGKTILHY MGTSTFSEYT VVADISVAKI DPLAPLDKVC LLGCGISTGY
GAAVNTAKLE PGSVCAVFGL GGVGLAVIMG CKVAGASRII GVDINKDKFA RAKEFGATEC
INPQDFSKPI QEVLIEMTDG GVDYSFECIG NVKVMRAALE ACHKGWGVSV VVGVAASGEE
IATRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTHNL SFDEINKAFE
LMHSGKSIRT VVKI
