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Database: UniProt
Entry: C3N212_SULIA
LinkDB: C3N212_SULIA
Original site: C3N212_SULIA 
ID   C3N212_SULIA            Unreviewed;       347 AA.
AC   C3N212;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=Alcohol dehydrogenase GroES domain protein {ECO:0000313|EMBL:ACP54422.1};
GN   OrderedLocusNames=M1627_0408 {ECO:0000313|EMBL:ACP54422.1};
OS   Sulfolobus islandicus (strain M.16.27).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=427318 {ECO:0000313|EMBL:ACP54422.1, ECO:0000313|Proteomes:UP000002307};
RN   [1] {ECO:0000313|EMBL:ACP54422.1, ECO:0000313|Proteomes:UP000002307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.27 {ECO:0000313|EMBL:ACP54422.1,
RC   ECO:0000313|Proteomes:UP000002307};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         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; CP001401; ACP54422.1; -; Genomic_DNA.
DR   RefSeq; WP_012710543.1; NC_012632.1.
DR   AlphaFoldDB; C3N212; -.
DR   GeneID; 84057920; -.
DR   KEGG; sim:M1627_0408; -.
DR   HOGENOM; CLU_026673_11_2_2; -.
DR   OMA; CERQTQP; -.
DR   Proteomes; UP000002307; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05284; arabinose_DH_like; 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; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 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; 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|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..345
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   347 AA;  37625 MW;  2AF34B458059007E CRC64;
     MRAVRLVEIG KPLVLKDIDI PKPKGAQVLI KVEAAGVCHS DVHMRQGRFG NLRIVEDLGV
     KLPVTLGHEI AGKIEEMGDE VVGYSKGDLV AVNPWQGEGN CYYCRIGEEH LCDSPRWLGI
     NFDGAYAEYV LIPHYKYMYK LRRLNAVEAS PLTCSGITTY RAVRKASLDP TKTLVVVGAG
     GGLGTMAVQI AKAVGGATII GVDVREEAVE TAKRAGADYV INASVQDPLV EIRRITEGKG
     IDAVIDLNNS EKTLSVYPKA LAKQGKYIMV GLFGADLHFH APLITLSEIQ FVGSLVGNQS
     DFLGIMRLAE AGKVKPMITK TMKLEEANEA IDNLENFKAV GRQVLIP
//
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