ID C9Y4B4_CROTZ Unreviewed; 361 AA.
AC C9Y4B4;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Uncharacterized zinc-type alcohol dehydrogenase-like protein yahK {ECO:0000313|EMBL:CBA30849.1};
DE EC=1.1.1.2 {ECO:0000313|EMBL:CBA30849.1};
DE EC=1.1.1.255 {ECO:0000313|EMBL:CBA30849.1};
GN Name=yahK {ECO:0000313|EMBL:CBA30849.1};
GN OrderedLocusNames=Ctu_21200 {ECO:0000313|EMBL:CBA30849.1};
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA30849.1, ECO:0000313|Proteomes:UP000002069};
RN [1] {ECO:0000313|Proteomes:UP000002069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC {ECO:0000313|Proteomes:UP000002069};
RX PubMed=21037008; DOI=10.1128/JB.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(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}.
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DR EMBL; FN543093; CBA30849.1; -; Genomic_DNA.
DR AlphaFoldDB; C9Y4B4; -.
DR KEGG; ctu:CTU_21200; -.
DR PATRIC; fig|693216.3.peg.2002; -.
DR HOGENOM; CLU_026673_20_2_6; -.
DR Proteomes; UP000002069; Chromosome.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046029; F:mannitol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CBA30849.1}; Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 12..344
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 361 AA; 39308 MW; A135490EF5A34824 CRC64;
MTMKVLGYAA QSAEAPLAPF EFTRRAPRPD DVVLEILYCG VCHSDLHQAR NDWGFSQYPI
VPGHEIIGRV TAVGSDVKKF KPGDLAGIGC MVDSCRTCHP CRDGLEQYCL EGCIQTYNGI
DRHDGEFTFG GYSQIILASQ DFVLRLPEGL DLKGAAPLLC AGITTWSPLR HWNVDKGSRV
AVVGLGGLGH MAIKLAHALG ADVTLFTRSP GKEEDARRLG AHHVVLSEEQ SQMQQVAGHF
DLIIDTVPYA HDINPYLSTL KIDGTLVFVG LLGEVQPAVN TVPMIMGRRS VAGSCIGGIA
ETQEMLDFCA KHHISADVEV INIQEINEAW ERMLKSDVKY RFVIDMASLQ QGARLAPVTA
A
//
