ID A0A1U8D2J0_ALLSI Unreviewed; 375 AA.
AC A0A1U8D2J0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN Name=ADH1C {ECO:0000313|RefSeq:XP_014375477.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014375477.1};
RN [1] {ECO:0000313|RefSeq:XP_014375477.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001146};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR RefSeq; XP_014375477.1; XM_014519991.2.
DR AlphaFoldDB; A0A1U8D2J0; -.
DR STRING; 38654.A0A1U8D2J0; -.
DR GeneID; 102384590; -.
DR KEGG; asn:102384590; -.
DR CTD; 126; -.
DR eggNOG; KOG0022; Eukaryota.
DR InParanoid; A0A1U8D2J0; -.
DR OrthoDB; 1077476at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006066; P:alcohol metabolic process; IEA:UniProt.
DR CDD; cd08299; alcohol_DH_class_I_II_IV; 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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF1; ALCOHOL DEHYDROGENASE 1A; 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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 22..373
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 375 AA; 39805 MW; 1B47278E82425D3B CRC64;
MSTAGKVIKC KAAITWEIKK PFSIEEIEVA PPKAHEVRIK ILATGICRSD DHVTAGLLTM
PLPMILGHEA AGVVESTGEG VTSLKPGDKV IPLFVPQCGE CMPCLKSNGN LCIRNDLGSP
SGLMADGTSR FTCKGKMIHH FIGTSTFTEY TVVHETAVAK IDAAAPLEKV CLIGCGFSTG
YGAAVKTAKV EPGSTCAVFG LGGVGLSTVM GCKAAGASRI IGIDINKDKF AKAKELGATE
CINPLDCKKP IQEVLSEMTG GGVDYSFEVI GRIDTMTAAL ACCQDNYGTC VIVGVPPASE
KITFNPMMLF TGRTWKGSVF GGWKSKESVP KLVADYMEKK INLDGLITHT LPFDKINEGF
ELLRKGKSIR SVLTF
//
