ID B7LPX9_ESCF3 Unreviewed; 387 AA.
AC B7LPX9;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Alcohol dehydrogenase, NAD(P)-dependent {ECO:0000313|EMBL:CAQ90444.1};
GN Name=yqhD {ECO:0000313|EMBL:CAQ90444.1};
GN OrderedLocusNames=EFER_2951 {ECO:0000313|EMBL:CAQ90444.1};
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054 {ECO:0000313|EMBL:CAQ90444.1, ECO:0000313|Proteomes:UP000000745};
RN [1] {ECO:0000313|Proteomes:UP000000745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 /
RC JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73
RC {ECO:0000313|Proteomes:UP000000745};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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DR EMBL; CU928158; CAQ90444.1; -; Genomic_DNA.
DR RefSeq; WP_001058836.1; NC_011740.1.
DR AlphaFoldDB; B7LPX9; -.
DR GeneID; 75060429; -.
DR KEGG; efe:EFER_2951; -.
DR HOGENOM; CLU_007207_0_4_6; -.
DR OrthoDB; 9815791at2; -.
DR Proteomes; UP000000745; Chromosome.
DR GO; GO:1990362; F:butanol dehydrogenase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd08187; BDH; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR044731; BDH-like.
DR PANTHER; PTHR43633; ALCOHOL DEHYDROGENASE YQHD; 1.
DR PANTHER; PTHR43633:SF1; ALCOHOL DEHYDROGENASE YQHD; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 9..360
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 387 AA; 42200 MW; 02C71923C140C5C3 CRC64;
MNNFNLHTPT RILFGKGAIA GLRNQIPQGA RVLITYGGGS VKKTGVLDQV LDALKGMDVL
EFGGIEPNPS YETLMKAVKL VREENVTFLL AVGGGSVLDG TKFIAAAAHY PDDIDPWHIL
ETGGKEIKSA IPMGSVLTLP ATGSESNAGA VISRKTTGDK QAFHSSHVQP VFAVLDPVYT
YTLPPRQVAN GVVDAFVHTV EQYVTYPVDG KIQDRFAEGI LLTLIEEGPK ALKEPENYDV
RANVMWAATQ ALNGLIGAGV PQDWATHMLG HELTAMHGLD HAQTLAIVLP ALWNEKRDTK
REKLLQYAER VWNITEGSDD ERIDAAIAAT RHFFEQMGVP THLSDYGLDG SSIPALLKKL
EEHGMTKLGE HHDITLDVSR RIYEAAR
//
