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Database: UniProt
Entry: W0JXZ9_9EURY
LinkDB: W0JXZ9_9EURY
Original site: W0JXZ9_9EURY 
ID   W0JXZ9_9EURY            Unreviewed;       287 AA.
AC   W0JXZ9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Alcohol dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HALLA_01915 {ECO:0000313|EMBL:AHG02085.1};
OS   Halostagnicola larsenii XH-48.
OG   Plasmid unnamed {ECO:0000313|EMBL:AHG02085.1}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halostagnicola.
OX   NCBI_TaxID=797299 {ECO:0000313|EMBL:AHG02085.1, ECO:0000313|Proteomes:UP000019024};
RN   [1] {ECO:0000313|EMBL:AHG02085.1, ECO:0000313|Proteomes:UP000019024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH-48 {ECO:0000313|EMBL:AHG02085.1,
RC   ECO:0000313|Proteomes:UP000019024};
RC   PLASMID=2 {ECO:0000313|Proteomes:UP000019024};
RG   DOE Joint Genome Institute;
RA   Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CP007057; AHG02085.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0JXZ9; -.
DR   KEGG; hlr:HALLA_01915; -.
DR   eggNOG; arCOG01459; Archaea.
DR   HOGENOM; CLU_026673_11_0_2; -.
DR   Proteomes; UP000019024; Plasmid 2.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051262; P:protein tetramerization; IEA:UniProt.
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; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Plasmid {ECO:0000313|EMBL:AHG02085.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019024};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          1..74
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          114..245
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   287 AA;  30027 MW;  0EC42B8877E68AED CRC64;
     MGHEVGGTVV EVGDDVDIEI GTEIVLNPLV ACEECSCCEE SKYNLCRDLQ VIGAQRPGAY
     AERVTAPASN VVPLPDGVSP QAAAVSEPVT VAFHAVMQSP LRDGHSVAVI GLGPIGLGLV
     QLVKAAGAGP IFASGHREAR RELAAECGAD VVIDPRETDP IEQIRSKTDG GVDVAFEMAG
     RESALNDAIN ATKPGGHTTL VGVFEDDVEI DPMDLVNNER SVNASAAYRT GPHADRDFSA
     VLEKFATGEI DHEPLVTSRI GLEDIVDDGF EALANADSGE VKVLVQP
//
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