ID A0A0J7Y1C3_9SPHN Unreviewed; 364 AA.
AC A0A0J7Y1C3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KMS57721.1};
GN ORFNames=V473_05805 {ECO:0000313|EMBL:KMS57721.1};
OS Sphingobium cupriresistens LL01.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1420583 {ECO:0000313|EMBL:KMS57721.1, ECO:0000313|Proteomes:UP000052232};
RN [1] {ECO:0000313|EMBL:KMS57721.1, ECO:0000313|Proteomes:UP000052232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL01 {ECO:0000313|EMBL:KMS57721.1,
RC ECO:0000313|Proteomes:UP000052232};
RX PubMed=25850427; DOI=10.1534/g3.114.015933;
RA Pearce S.L., Oakeshott J.G., Pandey G.;
RT "Insights into Ongoing Evolution of the Hexachlorocyclohexane Catabolic
RT Pathway from Comparative Genomics of Ten Sphingomonadaceae Strains.";
RL G3 (Bethesda) 5:1081-1094(2015).
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|RuleBase:RU361277}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMS57721.1}.
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DR EMBL; JACT01000001; KMS57721.1; -; Genomic_DNA.
DR RefSeq; WP_066601353.1; NZ_KQ130434.1.
DR AlphaFoldDB; A0A0J7Y1C3; -.
DR STRING; 1420583.V473_05805; -.
DR PATRIC; fig|1420583.3.peg.1169; -.
DR Proteomes; UP000052232; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08279; Zn_ADH_class_III; 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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000052232};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..361
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 364 AA; 38289 MW; 6D983FA89CDE58C2 CRC64;
MKAAILNSLD GSFQIEEIDI DAPRGREVLV EVKASGLCHS DLHFAEQDFG VPLPAVLGHE
LAGVVLAIGP EVREFVVGDH VVGSLIQFCG HCRACIGGRT YQCTHPEETL RDDPDHAHRL
TRNGEGVAQV FGTGAFAERA LVHENQLAKV PKELPFAQAS LLGCGTITGA GAAINTASVR
PGDTVAVIGI GGVGLNVISG AQLAGAARIV AIDMQPKKEE LARKFGATDF IDASAGDSVA
AVQALIEGGV DHAFEVVGIK ATSEQAIKMV RKGGGAYLIG VHSPANTIDV NVTIDLLTNQ
VDLRGVYMGS SNIKHDIPMY AQLYLEGKLN LDDLISREIN LADINDAYKE LKGGAIARSV
ITSF
//
