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Database: UniProt
Entry: C1B5F4_RHOOB
LinkDB: C1B5F4_RHOOB
Original site: C1B5F4_RHOOB 
ID   C1B5F4_RHOOB            Unreviewed;       354 AA.
AC   C1B5F4;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   SubName: Full=Putative zinc-containing alcohol dehydrogenase {ECO:0000313|EMBL:BAH51080.1};
DE            EC=1.1.1.- {ECO:0000313|EMBL:BAH51080.1};
GN   OrderedLocusNames=ROP_28330 {ECO:0000313|EMBL:BAH51080.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH51080.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH51080.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH51080.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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DR   EMBL; AP011115; BAH51080.1; -; Genomic_DNA.
DR   RefSeq; WP_012690036.1; NC_012522.1.
DR   AlphaFoldDB; C1B5F4; -.
DR   STRING; 632772.ROP_28330; -.
DR   KEGG; rop:ROP_28330; -.
DR   PATRIC; fig|632772.20.peg.2958; -.
DR   HOGENOM; CLU_026673_11_5_11; -.
DR   OMA; FILGHEC; -.
DR   OrthoDB; 9797931at2; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd08232; idonate-5-DH; 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; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43161:SF9; SORBITOL 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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:BAH51080.1}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          25..352
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   354 AA;  36156 MW;  887FEDD1676E291E CRC64;
     MSTSVHESGA ALPAETLGVV AHAAGDLRIE SVPLRRPESS EAVVEIAYGG ICGSDLHYWT
     HGAAGESILK APMLLGHEVV GTVVEAAADG TGPAAGDTVA VHPATPGGRG ARFPEDRPNL
     SPGCTYLGSA AQFPHTEGAF AKYAVLPSRM LRRLPANLPL RTAAVAEPAA VAWHAVARAG
     RVEGKSALVV GCGPIGALVV AVLRRAGARE ITAVDVHEYP RTVARALGAD TTLDATDAES
     IAAVDADIVV ECSGNRFGLE SAIRGATRGG RIVLLGLLPT GLQPAPLSLV ITRELELAGS
     FRFNDEIDAV LAALADGSLN VGPVISHEFG IADALEAFAV AKDASTSAKV LLAF
//
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