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ADHH_GADMO
ID   ADHH_GADMO              Reviewed;         375 AA.
AC   P81600;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Alcohol dehydrogenase class-3 chain H;
DE            EC=1.1.1.1 {ECO:0000250|UniProtKB:P11766};
DE   AltName: Full=Alcohol dehydrogenase class-III chain H;
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:0000250|UniProtKB:P11766};
OS   Gadus morhua (Atlantic cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX   NCBI_TaxID=8049;
RN   [1]
RP   PROTEIN SEQUENCE, SUBUNIT, AND ACETYLATION AT ALA-1.
RX   PubMed=8931553; DOI=10.1021/bi9618124;
RA   Danielsson O., Shafqat J., Estonius M., El-Ahmad M., Joernvall H.;
RT   "Isozyme multiplicity with anomalous dimer patterns in a class III alcohol
RT   dehydrogenase. Effects on the activity and quaternary structure of residue
RT   exchanges at 'non-functional' sites in a native protein.";
RL   Biochemistry 35:14561-14568(1996).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RX   PubMed=7607314; DOI=10.1016/0014-5793(95)00572-q;
RA   Hjelmqvist L., Hackett M., Shafqat J., Danielsson O., Iida J.,
RA   Hendrickson R.C., Michel H., Shabanowitz J., Hunt D.F., Joernvall H.;
RT   "Multiplicity of N-terminal structures of medium-chain alcohol
RT   dehydrogenases. Mass-spectrometric analysis of plant, lower vertebrate and
RT   higher vertebrate class I, II, and III forms of the enzyme.";
RL   FEBS Lett. 367:237-240(1995).
CC   -!- FUNCTION: Class-III ADH is remarkably ineffective in oxidizing ethanol,
CC       but it readily catalyzes the oxidation of long-chain primary alcohols
CC       and the oxidation of S-(hydroxymethyl) glutathione.
CC       {ECO:0000250|UniProtKB:P11766}.
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:0000250|UniProtKB:P11766};
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:0000250|UniProtKB:P11766};
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:0000250|UniProtKB:P11766};
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:0000250|UniProtKB:P11766};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P11766};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P11766};
CC   -!- SUBUNIT: Homodimer or heterodimer with L chain.
CC       {ECO:0000269|PubMed:8931553}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P81600; -.
DR   SMR; P81600; -.
DR   STRING; 8049.ENSGMOP00000013292; -.
DR   iPTMnet; P81600; -.
DR   Proteomes; UP000694546; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
DR   GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
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   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 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   Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..375
FT                   /note="Alcohol dehydrogenase class-3 chain H"
FT                   /id="PRO_0000160763"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P11766"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P11766"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11766"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11766"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11766"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11766"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P11766"
FT   SITE            116
FT                   /note="Important for FDH activity and activation by fatty
FT                   acids"
FT                   /evidence="ECO:0000250|UniProtKB:P11766"
FT   MOD_RES         1
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:7607314,
FT                   ECO:0000269|PubMed:8931553"
SQ   SEQUENCE   375 AA;  39669 MW;  0B9760AB77329FE3 CRC64;
     ATAGQVIKCK AAVAWEAGKP LSLEEVEVAP PRAGEVRIKV VATGVCHTDA YTLSGSDPEG
     AFPVILGHEG AGLVESVGEG VTKFKAGDTV IPLYVPQCGE CKFCKNPKTN LCQKIRVTQG
     RGLMPDNTSR FTCKGKQLFH FMGTSTFSEY TVVADISLAN VDPKAPLDKV CLLGCGISTG
     YGAALNTAKV EPGSTCAVFG LGAVGLAAIM GCKVAGATRI IGVDINPEKF GKAAEFGATE
     CLNPKDHARP VQEVLVEMTD GGVDYSFECI GNVEIMRSAL EACHKGWGES VIIGVAGAGQ
     EIATRPFQLV TGRVWKATAF GGWKSVESVP KLVEDYMNKK LKVDEFVTHT LPFDSINEGF
     DLMHAGKSIR CVLTF
 
 
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