ID Q0RVL1_RHOJR Unreviewed; 347 AA.
AC Q0RVL1;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=Zn-dependent alcohol dehydrogenase {ECO:0000313|EMBL:ABH00675.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:ABH00675.1};
GN OrderedLocusNames=RHA1_ro11028 {ECO:0000313|EMBL:ABH00675.1};
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL3 {ECO:0000313|EMBL:ABH00675.1,
OG ECO:0000313|Proteomes:UP000008710}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABH00675.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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|RuleBase:RU361277}.
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DR EMBL; CP000434; ABH00675.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0RVL1; -.
DR KEGG; rha:RHA1_ro11028; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_11; -.
DR Proteomes; UP000008710; Plasmid pRHL3.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; 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 InterPro; IPR020843; PKS_ER.
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 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABH00675.1}; Plasmid {ECO:0000313|EMBL:ABH00675.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..342
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 347 AA; 37082 MW; 31D45A696051AEB9 CRC64;
MKAAVYQRPG LIEVQDVPTP QPGPRDVLLR TRAVGICGSD LHVYRKGLYG ATTGWIMGHE
FCGEAVEVGE EVRGASVGER YTGFSVEFCG QCYWCQRNQQ RLCPHLFEHY TGYGEPGAMA
EYVLIRQAQL DQNLFAIPAS LSDEAAALAE PLGTAAYSVR RAKPQDGDTV VVIGGGMIGN
LIVQTVKATV DAKVIVTEVS PERAELALRV GADEVIDARR PDLIDAVRAA TGRGRYMFGD
SGMADVVFNA AAAPPTYAQS LDFVRSRGTV VLVGLSEEPA TADFSLIAYK DIRLIGAIGS
SISSGIELLE QGRVQVDALV TNRIPLSEAN SAFHQAADPT SIKGVPP
//
