YQHD_ECOLI
ID YQHD_ECOLI Reviewed; 387 AA.
AC Q46856; Q2M9I8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Alcohol dehydrogenase YqhD;
DE EC=1.1.1.2 {ECO:0000269|PubMed:15327949};
GN Name=yqhD; OrderedLocusNames=b3011, JW2978;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-387 IN COMPLEX WITH ZINC IONS
RP AND NADP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=15327949; DOI=10.1016/j.jmb.2004.07.034;
RA Sulzenbacher G., Alvarez K., Van Den Heuvel R.H., Versluis C., Spinelli S.,
RA Campanacci V., Valencia C., Cambillau C., Eklund H., Tegoni M.;
RT "Crystal structure of E.coli alcohol dehydrogenase YqhD: evidence of a
RT covalently modified NADP coenzyme.";
RL J. Mol. Biol. 342:489-502(2004).
CC -!- FUNCTION: NADP-dependent ADH activity. {ECO:0000269|PubMed:15327949}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH;
CC Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2;
CC Evidence={ECO:0000269|PubMed:15327949};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:15327949};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15327949}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; U28377; AAA69178.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76047.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77068.1; -; Genomic_DNA.
DR PIR; A65088; A65088.
DR RefSeq; NP_417484.1; NC_000913.3.
DR RefSeq; WP_001058802.1; NZ_SSZK01000023.1.
DR PDB; 1OJ7; X-ray; 2.00 A; A/B/C/D=2-387.
DR PDB; 4QGS; X-ray; 1.70 A; A=1-387.
DR PDBsum; 1OJ7; -.
DR PDBsum; 4QGS; -.
DR AlphaFoldDB; Q46856; -.
DR SMR; Q46856; -.
DR BioGRID; 4262380; 40.
DR DIP; DIP-12870N; -.
DR IntAct; Q46856; 3.
DR STRING; 511145.b3011; -.
DR DrugBank; DB02319; 5,6-dihydroxy-NADP.
DR jPOST; Q46856; -.
DR PaxDb; Q46856; -.
DR PRIDE; Q46856; -.
DR EnsemblBacteria; AAC76047; AAC76047; b3011.
DR EnsemblBacteria; BAE77068; BAE77068; BAE77068.
DR GeneID; 58459894; -.
DR GeneID; 947493; -.
DR KEGG; ecj:JW2978; -.
DR KEGG; eco:b3011; -.
DR PATRIC; fig|1411691.4.peg.3718; -.
DR EchoBASE; EB2834; -.
DR eggNOG; COG1979; Bacteria.
DR HOGENOM; CLU_007207_0_4_6; -.
DR InParanoid; Q46856; -.
DR OMA; CTMALNG; -.
DR PhylomeDB; Q46856; -.
DR BioCyc; EcoCyc:G7564-MON; -.
DR BioCyc; MetaCyc:G7564-MON; -.
DR BRENDA; 1.1.1.2; 2026.
DR SABIO-RK; Q46856; -.
DR EvolutionaryTrace; Q46856; -.
DR PRO; PR:Q46856; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:EcoCyc.
DR GO; GO:0018455; F:alcohol dehydrogenase [NAD(P)+] activity; IDA:EcoliWiki.
DR GO; GO:1990362; F:butanol dehydrogenase activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:1990002; F:methylglyoxal reductase (NADPH-dependent, acetol producing); IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:EcoCyc.
DR CDD; cd08187; BDH; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR044731; BDH-like.
DR PANTHER; PTHR43633; PTHR43633; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; NADP; Oxidoreductase; Reference proteome;
KW Zinc.
FT CHAIN 1..387
FT /note="Alcohol dehydrogenase YqhD"
FT /id="PRO_0000087832"
FT BINDING 38..40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15327949"
FT BINDING 93..99
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15327949"
FT BINDING 138
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15327949"
FT BINDING 147
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15327949"
FT BINDING 160
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15327949"
FT BINDING 179..182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15327949"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15327949,
FT ECO:0007744|PDB:1OJ7"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15327949,
FT ECO:0007744|PDB:1OJ7"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15327949,
FT ECO:0007744|PDB:1OJ7"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15327949,
FT ECO:0007744|PDB:1OJ7"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:4QGS"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:4QGS"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:4QGS"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:4QGS"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:4QGS"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:4QGS"
FT TURN 122..126
FT /evidence="ECO:0007829|PDB:4QGS"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1OJ7"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:4QGS"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:1OJ7"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4QGS"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:4QGS"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 185..200
FT /evidence="ECO:0007829|PDB:4QGS"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:4QGS"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1OJ7"
FT HELIX 211..233
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:4QGS"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1OJ7"
FT TURN 255..259
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 281..295
FT /evidence="ECO:0007829|PDB:4QGS"
FT TURN 296..300
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 301..312
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 319..336
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 353..362
FT /evidence="ECO:0007829|PDB:4QGS"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:4QGS"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:4QGS"
FT HELIX 376..385
FT /evidence="ECO:0007829|PDB:4QGS"
SQ SEQUENCE 387 AA; 42097 MW; 448A7610787D2146 CRC64;
MNNFNLHTPT RILFGKGAIA GLREQIPHDA RVLITYGGGS VKKTGVLDQV LDALKGMDVL
EFGGIEPNPA YETLMNAVKL VREQKVTFLL AVGGGSVLDG TKFIAAAANY PENIDPWHIL
QTGGKEIKSA IPMGCVLTLP ATGSESNAGA VISRKTTGDK QAFHSAHVQP VFAVLDPVYT
YTLPPRQVAN GVVDAFVHTV EQYVTKPVDA KIQDRFAEGI LLTLIEDGPK ALKEPENYDV
RANVMWAATQ ALNGLIGAGV PQDWATHMLG HELTAMHGLD HAQTLAIVLP ALWNEKRDTK
RAKLLQYAER VWNITEGSDD ERIDAAIAAT RNFFEQLGVP THLSDYGLDG SSIPALLKKL
EEHGMTQLGE NHDITLDVSR RIYEAAR
