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ADHX_MYXGL
ID   ADHX_MYXGL              Reviewed;         376 AA.
AC   P80360;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Alcohol dehydrogenase class-3;
DE            EC=1.1.1.1 {ECO:0000250|UniProtKB:P11766};
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:0000250|UniProtKB:P11766};
OS   Myxine glutinosa (Atlantic hagfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata; Myxini;
OC   Myxiniformes; Myxinidae; Myxininae; Myxine.
OX   NCBI_TaxID=7769;
RN   [1]
RP   PROTEIN SEQUENCE, TISSUE SPECIFICITY, AND ACETYLATION AT SER-1.
RC   TISSUE=Liver;
RX   PubMed=7957198; DOI=10.1111/j.1432-1033.1994.1081b.x;
RA   Danielsson O., Shafqat J., Estonius M., Joernvall H.;
RT   "Alcohol dehydrogenase class III contrasted to class I. Characterization of
RT   the cyclostome enzyme, the existence of multiple forms as for the human
RT   enzyme, and distant cross-species hybridization.";
RL   Eur. J. Biochem. 225:1081-1088(1994).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT SER-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. {ECO:0000250|UniProtKB:P11766}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Liver and gut. {ECO:0000269|PubMed:7957198}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily. {ECO:0000305}.
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DR   PIR; S51187; S51187.
DR   AlphaFoldDB; P80360; -.
DR   SMR; P80360; -.
DR   iPTMnet; P80360; -.
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; Zinc.
FT   CHAIN           1..376
FT                   /note="Alcohol dehydrogenase class-3"
FT                   /id="PRO_0000160765"
FT   BINDING         47
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         69
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         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11766"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11766"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11766"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11766"
FT   BINDING         176
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            117
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-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:7607314,
FT                   ECO:0000269|PubMed:7957198"
SQ   SEQUENCE   376 AA;  39747 MW;  FFD20C195FF67B5F CRC64;
     SKMDGQVIHC KAAVAWEAKK PLSLEEIEVA PPKAHEVRMK VLATAVCHTD AYTLSGVDPE
     GSFPVVLGHE GAGIVESVGE GVTKFKPGDS VIPLYIPQCG ECKFCLNPKT NLCQKIRVTQ
     GKGMMPDGTS RLTCRGKSLY HFMGASTFSE YAVVADISLC RVAPEAPPDR VCLLGCGVST
     GYGAPLNTAK VEPGSTCAIF GLGAVGLAAI MGCRVAGASR IIAIDRNPDK FEKARIFGAT
     DCVVPDASDK PISQVLGEMT DGGLDYTFEC VGNVGIMRAA LESCHKGWGV SVILGVAGGG
     QEISTRPFQL VTGRTWKGAA FGGWKSVESV PKLVDDYMAG KIMVDEFVSH SLPFDSINEA
     FDLMHAGKSI RTVLQL
 
 
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