ID Q8KLT9_9NOCA Unreviewed; 346 AA.
AC Q8KLT9;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 125.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN Name=sadh {ECO:0000313|EMBL:CAD36475.1};
GN ORFNames=RHRU231_470141 {ECO:0000313|EMBL:CDZ89293.1};
OS Rhodococcus ruber.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1830 {ECO:0000313|EMBL:CAD36475.1};
RN [1] {ECO:0000313|EMBL:CAD36475.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=219 {ECO:0000313|EMBL:CAD36475.1};
RA Tamak C., Plattner H., Hummel W., Diekmann H., Meens J.;
RT "Thermostable NAD+-dependent medium-chain alcohol dehydrogenase in
RT tetrahydrofuran metabolism in Rhodococcus ruber strain 219.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-345 IN COMPLEX WITH NAD AND
RP ZINC.
RX PubMed=20676439; DOI=10.1039/c0cc00929f;
RA Karabec M., Lyskowski A., Tauber K.C., Steinkellner G., Kroutil W.,
RA Grogan G., Gruber K.;
RT "Structural insights into substrate specificity and solvent tolerance in
RT alcohol dehydrogenase ADH-'A' from Rhodococcus ruber DSM 44541.";
RL Chem. Commun. (Camb.) 46:6314-6316(2010).
RN [3] {ECO:0000313|EMBL:CDZ89293.1, ECO:0000313|Proteomes:UP000042997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ivshina I.B., Kuyukina M.S., Krivoruchko A.V., Barbe V., Fischer C.;
RT "Draft Genome Sequence of Propane- and Butane-Oxidizing Actinobacterium
RT Rhodococcus ruber IEGM 231.";
RL Genome Announc. 2:1-2(2014).
RN [4] {ECO:0000313|EMBL:CDZ89293.1}
RP NUCLEOTIDE SEQUENCE.
RA Regsiter Alias;
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ491307; CAD36475.1; -; Genomic_DNA.
DR EMBL; CCSD01000058; CDZ89293.1; -; Genomic_DNA.
DR RefSeq; WP_010594839.1; NZ_LRRL01000063.1.
DR PDB; 2XAA; X-ray; 2.80 A; A/B/C/D=1-345.
DR PDB; 3JV7; X-ray; 2.00 A; A/B/C/D=1-345.
DR PDBsum; 2XAA; -.
DR PDBsum; 3JV7; -.
DR GeneID; 66836808; -.
DR KEGG; rrz:CS378_07205; -.
DR eggNOG; COG1064; Bacteria.
DR OrthoDB; 3567264at2; -.
DR BRENDA; 1.1.1.1; 4359.
DR Proteomes; UP000042997; Unassembled WGS sequence.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7};
KW Metal-binding {ECO:0000256|RuleBase:RU361277, ECO:0007829|PDB:2XAA};
KW Nucleotide-binding {ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAD36475.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000042997};
KW Zinc {ECO:0000256|RuleBase:RU361277, ECO:0007829|PDB:2XAA}.
FT DOMAIN 10..343
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:2XAA"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 293
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
FT BINDING 340
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:2XAA, ECO:0007829|PDB:3JV7"
SQ SEQUENCE 346 AA; 35449 MW; F885D8B0F7E6C1CC CRC64;
MKALQYTEIG SEPVVVDVPT PAPGPGEILL KVTAAGLCHS DIFVMDMPAE QYIYGLPLTL
GHEGVGTVAE LGAGVTGFET GDAVAVYGPW GCGACHACAR GRENYCTRAA ELGITPPGLG
SPGSMAEYMI VDSARHLVPI GDLDPVAAVP LTDAGLTPYH AISRVLPLLG PGSTAVVIGV
GGLGHVGIQI LRAVSAARVI AVDLDDDRLA LAREVGADAA VKSGAGAADA IRELTGGEGA
TAVFDFVGAQ STIDTAQQVV AIDGHISVVG IHAGAHAKVG FFMIPFGASV VTPYWGTRSE
LMDVVDLARA GRLDIHTETF TLDEGPTAYR RLREGSIRGR GVVVPG
//