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 13-SEP-2023, entry version 112.
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 Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR014183; ADH_3.
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 NCBIfam; TIGR02818; adh_III_F_hyde; 1.
DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//
