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Database: UniProt
Entry: Q6FBY3_ACIAD
LinkDB: Q6FBY3_ACIAD
Original site: Q6FBY3_ACIAD 
ID   Q6FBY3_ACIAD            Unreviewed;       371 AA.
AC   Q6FBY3;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 134.
DE   SubName: Full=Putative aryl-alcohol dehydrogenase (Benzyl alcohol dehydrogenase) (XylB-like) {ECO:0000313|EMBL:CAG68428.1};
DE            EC=1.1.1.90 {ECO:0000313|EMBL:CAG68428.1};
GN   OrderedLocusNames=ACIAD1578 {ECO:0000313|EMBL:CAG68428.1};
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG68428.1, ECO:0000313|Proteomes:UP000000430};
RN   [1] {ECO:0000313|EMBL:CAG68428.1, ECO:0000313|Proteomes:UP000000430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC         Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000781};
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}.
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DR   EMBL; CR543861; CAG68428.1; -; Genomic_DNA.
DR   RefSeq; WP_004925126.1; NC_005966.1.
DR   AlphaFoldDB; Q6FBY3; -.
DR   STRING; 202950.GCA_001485005_02003; -.
DR   GeneID; 45233968; -.
DR   KEGG; aci:ACIAD1578; -.
DR   eggNOG; COG1062; Bacteria.
DR   HOGENOM; CLU_026673_14_1_6; -.
DR   OMA; RGQFFGQ; -.
DR   OrthoDB; 9805663at2; -.
DR   BioCyc; ASP62977:ACIAD_RS07235-MONOMER; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0018456; F:aryl-alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08278; benzyl_alcohol_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; 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; 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   ECO:0000313|EMBL:CAG68428.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000430};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..364
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   371 AA;  39508 MW;  B8E1A9568169D0B8 CRC64;
     MKITAAVARQ AHQDFSIEQV ELDEPKDHEV LVRIEGVGLC HTDLVARDRL IPIPLPAVLG
     HEGAGVVEKI GKAVTKVAVG DHVLMSFNSC GECPRCKEHL PPYCTQFPQL NYVGARPDGS
     STLKQNDQAV SGYFFGQSSF ASHALANERN IVKVAQDLPI EILGPLGCGL QTGAGGVMRS
     LACPQGSTIA IFGGGPVGLA AVMGAVIQQC ATIILVEPMA SRRELALELG AHHVIDPAQG
     NITEHIRNIL PQGVDFAFES SGRGEVVEAA LASLGSHGLL GLVGVPPSVE TTLNVNLVSL
     ITFGHRIHGI IEGDSDLDTF LPELIQHYQA GKFPFDKLIK KYALSEINQA IQDQAQGRCI
     KAVLIPEHAH H
//
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