ID A0A060QBQ4_9PROT Unreviewed; 332 AA.
AC A0A060QBQ4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN ORFNames=ASAP_0539 {ECO:0000313|EMBL:CDG38584.1};
OS Asaia bogorensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Asaia.
OX NCBI_TaxID=91915 {ECO:0000313|EMBL:CDG38584.1, ECO:0000313|Proteomes:UP000027583};
RN [1] {ECO:0000313|EMBL:CDG38584.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG38584.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24682158; DOI=10.1093/gbe/evu062;
RA Chouaia B., Gaiarsa S., Crotti E., Comandatore F., Degli Esposti M.,
RA Ricci I., Alma A., Favia G., Bandi C., Daffonchio D.;
RT "Acetic acid bacteria genomes reveal functional traits for adaptation to
RT life in insect guts.";
RL Genome Biol. Evol. 6:912-920(2014).
RN [2] {ECO:0000313|EMBL:CDG38584.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG38584.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24804722; DOI=10.1371/journal.pone.0096566;
RA Degli Esposti M., Chouaia B., Comandatore F., Crotti E., Sassera D.,
RA Lievens P.M., Daffonchio D., Bandi C.;
RT "Evolution of mitochondria reconstructed from the energy metabolism of
RT living bacteria.";
RL PLoS ONE 9:e96566-e96566(2014).
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|RuleBase:RU364000}.
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:CDG38584.1}.
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DR EMBL; CBLX010000004; CDG38584.1; -; Genomic_DNA.
DR RefSeq; WP_023977817.1; NZ_CBLX010000004.1.
DR AlphaFoldDB; A0A060QBQ4; -.
DR eggNOG; COG0604; Bacteria.
DR Proteomes; UP000027583; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08252; AL_MDR; 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; IPR014182; ADH_Zn_typ-1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR02817; adh_fam_1; 1.
DR PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 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 Lyase {ECO:0000313|EMBL:CDG38584.1};
KW Metal-binding {ECO:0000256|RuleBase:RU364000};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364000,
KW ECO:0000313|EMBL:CDG38584.1}; Zinc {ECO:0000256|RuleBase:RU364000}.
FT DOMAIN 13..330
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 332 AA; 36029 MW; 550D6A907DF3D9E8 CRC64;
MKAVGYKAPG APDVLQDITL PDPPAPKGHD LLVRVRAVSI NPVDTKIRVR AGALDGEAWR
VLGWDAAGIV EATGPEVRFF KPGDKVFYAG ALMRQGSNAE MQTVDERLVG HMPDRLDWGQ
AASLPLTSVT AWEMLFDRMA VTNLTKGVLL VVGGAGGVGS ILIQLARKLT GLTVIATASR
DETRDWVLRM GAHHVIDHRQ DMAAQIRALG FEQVTHIAAL TATDRHQAFY EEILAPQGHL
SVIDDPTHFD IVGFKKKSAT ISWEFMFTRS LFATPDQARQ HDILEQVSSL VQSGDVVATE
YHRAQGLSAA ALGRLHSESE SGKSIGKSVL VF
//
