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Database: UniProt
Entry: Q06XS9_COILA
LinkDB: Q06XS9_COILA
Original site: Q06XS9_COILA 
ID   Q06XS9_COILA            Unreviewed;       379 AA.
AC   Q06XS9;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 2.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Alcohol dehydrogenase 1 {ECO:0000256|ARBA:ARBA00041139};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
OS   Coix lacryma-jobi (Job's tears).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Rottboelliinae; Coix.
OX   NCBI_TaxID=4505 {ECO:0000313|EMBL:ABE68381.2};
RN   [1] {ECO:0000313|EMBL:ABE68381.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu G., Li Y., Chen D.;
RT   "Molecular cloning, nucleotide sequencing and expression of cDNA encoding
RT   alcohol dehydrogenases from Coix lacryma-jobi L. during waterlogging.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABE68381.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Chen D., Zhu Y., Li Y.;
RT   "Molecular cloning and prokaryotic expression of alcohol dehydrogenases
RT   cDNA from Coix.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ABE68381.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Chen D., Zhu Y., Li Y.;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:0000256|ARBA:ARBA00000781};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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   EMBL; DQ455071; ABE68381.2; -; mRNA.
DR   AlphaFoldDB; Q06XS9; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08301; alcohol_DH_plants; 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   PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF40; ALCOHOL DEHYDROGENASE 1; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          36..121
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          205..337
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   379 AA;  40965 MW;  4E265A2599F8A7C9 CRC64;
     MATAGKVIKC RAAVAWEASK PLSIEEVEVA PPQAMEVHVK ILFTSLCHTD VYFWEAKGQT
     PVFPRIFGHE AGGIVESVGE GVTDLAPGDH VLPVFTGECK ECAHCKSAES NMCDLLRINT
     DRGVMIGDGK SRFSINGKPI YHFVGTSTFS EYSVMHVGCV AKINPEAPLD KVCVLSCGIS
     TGLGASINVA KPPKGSTVAI FGLGAVGLAA AEGARIAGAS RIIGIDLNPN RFEEAKKFGC
     TEFVNPKDHN KPAQEVLAEM TNGGVDRSVE CTGNIHAMIQ AFECVHDGWG VAVLVGVPHK
     DAEFKTHPMN FLNERTLKGT FFGNYKPRTD LPNVVELYMK KELEVEKFIT HSVPFAEINK
     AFDLMAKGEG IRCIIRMEN
//
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