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Database: UniProt
Entry: ADHP_ECOLI
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Original site: ADHP_ECOLI 
ID   ADHP_ECOLI              Reviewed;         336 AA.
AC   P39451; P76126; P78157; P78268;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 164.
DE   RecName: Full=Alcohol dehydrogenase, propanol-preferring;
DE            EC=1.1.1.1;
GN   Name=adhP; Synonyms=yddN; OrderedLocusNames=b1478, JW1474;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-35, AND CHARACTERIZATION.
RA   Harayama S.;
RL   Submitted (OCT-1994) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 87-118.
RX   PubMed=2158980; DOI=10.1128/jb.172.5.2774-2778.1990;
RA   Kubo K.M., Craig N.L.;
RT   "Bacterial transposon Tn7 utilizes two different classes of target sites.";
RL   J. Bacteriol. 172:2774-2778(1990).
CC   -!- FUNCTION: Preferred specificity is towards 1-propanol.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC         Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; U00096; AAC74551.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15126.1; -; Genomic_DNA.
DR   EMBL; M31532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A64901; A64901.
DR   RefSeq; NP_415995.4; NC_000913.3.
DR   RefSeq; WP_000642433.1; NZ_SSZK01000038.1.
DR   PDB; 4GKV; X-ray; 2.01 A; A/B/C/D=1-336.
DR   PDBsum; 4GKV; -.
DR   AlphaFoldDB; P39451; -.
DR   SMR; P39451; -.
DR   BioGRID; 4262899; 24.
DR   IntAct; P39451; 5.
DR   STRING; 511145.b1478; -.
DR   jPOST; P39451; -.
DR   PaxDb; 511145-b1478; -.
DR   EnsemblBacteria; AAC74551; AAC74551; b1478.
DR   GeneID; 946036; -.
DR   KEGG; ecj:JW1474; -.
DR   KEGG; eco:b1478; -.
DR   PATRIC; fig|1411691.4.peg.789; -.
DR   EchoBASE; EB2506; -.
DR   eggNOG; COG1064; Bacteria.
DR   HOGENOM; CLU_026673_20_1_6; -.
DR   InParanoid; P39451; -.
DR   OMA; GLKMTDT; -.
DR   OrthoDB; 9771084at2; -.
DR   PhylomeDB; P39451; -.
DR   BioCyc; EcoCyc:ADHP-MONOMER; -.
DR   BioCyc; MetaCyc:ADHP-MONOMER; -.
DR   PRO; PR:P39451; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:EcoCyc.
DR   GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR   GO; GO:0046187; P:acetaldehyde catabolic process; IDA:EcoliWiki.
DR   GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki.
DR   GO; GO:0045471; P:response to ethanol; IEP:EcoliWiki.
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   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Metal-binding; NAD;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..336
FT                   /note="Alcohol dehydrogenase, propanol-preferring"
FT                   /id="PRO_0000160740"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        34
FT                   /note="C -> P (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90
FT                   /note="G -> R (in Ref. 5; M31532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104
FT                   /note="R -> P (in Ref. 5; M31532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="N -> K (in Ref. 5; M31532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="S -> G (in Ref. 5; M31532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117..118
FT                   /note="MA -> RV (in Ref. 5; M31532)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          12..16
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          26..35
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           38..45
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          58..67
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          79..87
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          90..92
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   TURN            109..111
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          116..124
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           137..143
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           146..156
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          164..168
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           172..183
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          188..194
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           196..204
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          208..212
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   TURN            213..215
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           218..226
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          227..234
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           239..248
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          249..257
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          262..268
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           269..274
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          278..281
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           287..298
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          306..309
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           311..313
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   HELIX           314..322
FT                   /evidence="ECO:0007829|PDB:4GKV"
FT   STRAND          327..333
FT                   /evidence="ECO:0007829|PDB:4GKV"
SQ   SEQUENCE   336 AA;  35380 MW;  8A9080F273866947 CRC64;
     MKAAVVTKDH HVDVTYKTLR SLKHGEALLK MECCGVCHTD LHVKNGDFGD KTGVILGHEG
     IGVVAEVGPG VTSLKPGDRA SVAWFYEGCG HCEYCNSGNE TLCRSVKNAG YSVDGGMAEE
     CIVVADYAVK VPDGLDSAAA SSITCAGVTT YKAVKLSKIR PGQWIAIYGL GGLGNLALQY
     AKNVFNAKVI AIDVNDEQLK LATEMGADLA INSHTEDAAK IVQEKTGGAH AAVVTAVAKA
     AFNSAVDAVR AGGRVVAVGL PPESMSLDIP RLVLDGIEVV GSLVGTRQDL TEAFQFAAEG
     KVVPKVALRP LADINTIFTE MEEGKIRGRM VIDFRH
//
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