ID YDJJ_ECOLI Reviewed; 347 AA.
AC P77280; P78174;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 152.
DE RecName: Full=Uncharacterized zinc-type alcohol dehydrogenase-like protein YdjJ;
DE EC=1.-.-.-;
GN Name=ydjJ; OrderedLocusNames=b1774, JW1763;
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).
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; AAC74844.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15572.1; -; Genomic_DNA.
DR PIR; F64937; F64937.
DR RefSeq; NP_416288.1; NC_000913.3.
DR RefSeq; WP_000798110.1; NZ_SSZK01000001.1.
DR PDB; 5VM2; X-ray; 1.98 A; A/B=1-347.
DR PDBsum; 5VM2; -.
DR AlphaFoldDB; P77280; -.
DR SMR; P77280; -.
DR BioGRID; 4260306; 423.
DR IntAct; P77280; 9.
DR STRING; 511145.b1774; -.
DR jPOST; P77280; -.
DR PaxDb; 511145-b1774; -.
DR EnsemblBacteria; AAC74844; AAC74844; b1774.
DR GeneID; 946292; -.
DR KEGG; ecj:JW1763; -.
DR KEGG; eco:b1774; -.
DR PATRIC; fig|1411691.4.peg.480; -.
DR EchoBASE; EB3259; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_5_6; -.
DR InParanoid; P77280; -.
DR OMA; MRVAMYY; -.
DR OrthoDB; 9773078at2; -.
DR PhylomeDB; P77280; -.
DR BioCyc; EcoCyc:G6961-MONOMER; -.
DR PRO; PR:P77280; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05285; sorbitol_DH; 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 InterPro; IPR045306; SDH-like.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; SORBITOL DEHYDROGENASE; 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; Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..347
FT /note="Uncharacterized zinc-type alcohol dehydrogenase-like
FT protein YdjJ"
FT /id="PRO_0000160892"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
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 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 28..38
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:5VM2"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 145..163
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:5VM2"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 225..232
FT /evidence="ECO:0007829|PDB:5VM2"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 258..268
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:5VM2"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 324..333
FT /evidence="ECO:0007829|PDB:5VM2"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:5VM2"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:5VM2"
SQ SEQUENCE 347 AA; 37701 MW; F8E2172184626A3B CRC64;
MKNSKAILQV PGTMKIISAE IPVPKEDEVL IKVEYVGICG SDVHGFESGP FIPPKDPNQE
IGLGHECAGT VVAVGSRVRK FKPGDRVNIE PGVPCGHCRY CLEGKYNICP DVDFMATQPN
YRGALTHYLC HPESFTYKLP DNMDTMEGAL VEPAAVGMHA AMLADVKPGK KIIILGAGCI
GLMTLQACKC LGATEIAVVD VLEKRLAMAE QLGATVVING AKEDTIARCQ QFTEDMGADI
VFETAGSAVT VKQAPYLVMR GGKIMIVGTV PGDSAINFLK INREVTIQTV FRYANRYPVT
IEAISSGRFD VKSMVTHIYD YRDVQQAFEE SVNNKRDIIK GVIKISD
//
