ID F0BKU7_9XANT Unreviewed; 342 AA.
AC F0BKU7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=XVE_4914 {ECO:0000313|EMBL:EGD06905.1};
OS Xanthomonas vesicatoria ATCC 35937.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=925775 {ECO:0000313|EMBL:EGD06905.1, ECO:0000313|Proteomes:UP000003299};
RN [1] {ECO:0000313|EMBL:EGD06905.1, ECO:0000313|Proteomes:UP000003299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35937 {ECO:0000313|EMBL:EGD06905.1,
RC ECO:0000313|Proteomes:UP000003299};
RX PubMed=21396108; DOI=10.1186/1471-2164-12-146;
RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P.,
RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., Preston J.F.,
RA Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., Staskawicz B.J.,
RA Jones J.B.;
RT "Comparative genomics reveals diversity among xanthomonads infecting tomato
RT and pepper.";
RL BMC Genomics 12:146-146(2011).
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 -!- 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:EGD06905.1}.
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DR EMBL; AEQV01000274; EGD06905.1; -; Genomic_DNA.
DR RefSeq; WP_005998065.1; NZ_CP018725.1.
DR AlphaFoldDB; F0BKU7; -.
DR GeneID; 46982303; -.
DR KEGG; xve:BJD12_13140; -.
DR eggNOG; COG1064; Bacteria.
DR Proteomes; UP000003299; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08297; CAD3; 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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..338
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 342 AA; 35493 MW; 81543758E40B9B1A CRC64;
MDATMKAAVV RQFGAPLVIE EVPVPRPQAG DLLVRIQACG VCHTDLHAAQ GDWPVKPNPP
FIPGHEGVGY VVAVGAGVRH VKEGDRVGIP WLYSACGHCE HCLGGWETLC EAQQNSGYSV
NGGFAQYALA NADYVGHLPA TLGFVEVAPI LCAGVTVYKG LKMTDTKPGQ WVVISGIGGL
GHLAVQYARA MGLNVAAVDV DDGKLALARR LGAAVTVNAL TTDPVAALRK DIGGAHGALV
TAVSPKAFEQ AIGMVRRGGT VSLNGLPPGQ FPLDIVGMVL NGVTVRGSIV GTRLDLQESL
AFAEQGKVAA TVATDTLDNI NDVFARMHAG TIEGRIVLDM AA
//