PAAH_ECOLI
ID PAAH_ECOLI Reviewed; 475 AA.
AC P76083; O53016; P78289;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=3-hydroxyadipyl-CoA dehydrogenase {ECO:0000303|PubMed:20660314};
DE EC=1.1.1.- {ECO:0000269|PubMed:20660314};
GN Name=paaH; Synonyms=ydbU; OrderedLocusNames=b1395, JW1390;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PHENYLACETATE CATABOLISM,
RP AND INDUCTION.
RC STRAIN=W / ATCC 11105 / DSM 1900;
RX PubMed=9748275; DOI=10.1074/jbc.273.40.25974;
RA Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M.,
RA Garcia J.L., Diaz E.;
RT "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a
RT new aerobic hybrid pathway.";
RL J. Biol. Chem. 273:25974-25986(1998).
RN [2]
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 [3]
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 [4]
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 [5]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=10766858; DOI=10.1074/jbc.275.16.12214;
RA Ferrandez A., Garcia J.L., Diaz E.;
RT "Transcriptional regulation of the divergent paa catabolic operons for
RT phenylacetic acid degradation in Escherichia coli.";
RL J. Biol. Chem. 275:12214-12222(2000).
RN [6]
RP DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=12846838; DOI=10.1046/j.1432-1033.2003.03683.x;
RA Ismail W., El-Said Mohamed M., Wanner B.L., Datsenko K.A., Eisenreich W.,
RA Rohdich F., Bacher A., Fuchs G.;
RT "Functional genomics by NMR spectroscopy. Phenylacetate catabolism in
RT Escherichia coli.";
RL Eur. J. Biochem. 270:3047-3054(2003).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20660314; DOI=10.1073/pnas.1005399107;
RA Teufel R., Mascaraque V., Ismail W., Voss M., Perera J., Eisenreich W.,
RA Haehnel W., Fuchs G.;
RT "Bacterial phenylalanine and phenylacetate catabolic pathway revealed.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14390-14395(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 4-475, AND SUBUNIT.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of 3-hydroxybutyryl-CoA dehydrogenase from Escherichia
RT coli K12.";
RL Submitted (JUN-2010) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the oxidation of 3-hydroxyadipyl-CoA to yield 3-
CC oxoadipyl-CoA. {ECO:0000269|PubMed:20660314,
CC ECO:0000269|PubMed:9748275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxyadipyl-CoA + NAD(+) = 3-oxoadipyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:34851, ChEBI:CHEBI:15378, ChEBI:CHEBI:57348,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132183;
CC Evidence={ECO:0000269|PubMed:20660314};
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC {ECO:0000269|PubMed:12846838}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000305}.
CC -!- INDUCTION: Activated by cAMP receptor protein (CRP), integration host
CC factor (IHF) and by phenylacetyl-coenzyme A (PA-CoA) that prevents PaaX
CC from binding its target sequences. Inhibited by PaaX.
CC {ECO:0000269|PubMed:10766858, ECO:0000269|PubMed:9748275}.
CC -!- DISRUPTION PHENOTYPE: Mutants accumulate 3-hydroxyadipate and are
CC unable to use phenylacetate as a carbon source.
CC {ECO:0000269|PubMed:12846838}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X97452; CAA66097.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74477.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15001.2; -; Genomic_DNA.
DR PIR; F64890; F64890.
DR RefSeq; NP_415913.1; NC_000913.3.
DR RefSeq; WP_000973360.1; NZ_SSZK01000012.1.
DR PDB; 3MOG; X-ray; 2.20 A; A/B/C=4-475.
DR PDBsum; 3MOG; -.
DR AlphaFoldDB; P76083; -.
DR SMR; P76083; -.
DR BioGRID; 4259599; 406.
DR IntAct; P76083; 1.
DR STRING; 511145.b1395; -.
DR PaxDb; P76083; -.
DR PRIDE; P76083; -.
DR DNASU; 945940; -.
DR EnsemblBacteria; AAC74477; AAC74477; b1395.
DR EnsemblBacteria; BAA15001; BAA15001; BAA15001.
DR GeneID; 945940; -.
DR KEGG; ecj:JW1390; -.
DR KEGG; eco:b1395; -.
DR PATRIC; fig|511145.12.peg.1458; -.
DR EchoBASE; EB3505; -.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_2_2_6; -.
DR InParanoid; P76083; -.
DR OMA; HPVRLYD; -.
DR PhylomeDB; P76083; -.
DR BioCyc; EcoCyc:G6716-MON; -.
DR BioCyc; MetaCyc:G6716-MON; -.
DR UniPathway; UPA00930; -.
DR EvolutionaryTrace; P76083; -.
DR PRO; PR:P76083; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0008691; F:3-hydroxybutyryl-CoA dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0010124; P:phenylacetate catabolic process; IMP:UniProtKB.
DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR011967; 3-OHacyl-CoA_DH_PaaC.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR041040; 3HCDH_RFF.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00725; 3HCDH; 2.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF18321; 3HCDH_RFF; 1.
DR SUPFAM; SSF48179; SSF48179; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02279; PaaC-3OHAcCoADH; 1.
DR PROSITE; PS00067; 3HCDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..475
FT /note="3-hydroxyadipyl-CoA dehydrogenase"
FT /id="PRO_0000109332"
FT VARIANT 132
FT /note="I -> V (in strain: W)"
FT VARIANT 344
FT /note="I -> V (in strain: W)"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 38..53
FT /evidence="ECO:0007829|PDB:3MOG"
FT TURN 54..59
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:3MOG"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:3MOG"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:3MOG"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 239..252
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 330..337
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 348..356
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 362..373
FT /evidence="ECO:0007829|PDB:3MOG"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:3MOG"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:3MOG"
FT TURN 386..389
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 390..406
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 412..422
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 429..436
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 438..452
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:3MOG"
FT HELIX 461..470
FT /evidence="ECO:0007829|PDB:3MOG"
SQ SEQUENCE 475 AA; 51733 MW; DEB6190F08D527C6 CRC64;
MMINVQTVAV IGSGTMGAGI AEVAASHGHQ VLLYDISAEA LTRAIDGIHA RLNSRVTRGK
LTAETCERTL KRLIPVTDIH ALAAADLVIE AASERLEVKK ALFAQLAEVC PPQTLLTTNT
SSISITAIAA EIKNPERVAG LHFFNPAPVM KLVEVVSGLA TAAEVVEQLC ELTLSWGKQP
VRCHSTPGFI VNRVARPYYS EAWRALEEQV AAPEVIDAAL RDGAGFPMGP LELTDLIGQD
VNFAVTCSVF NAFWQERRFL PSLVQQELVI GGRLGKKSGL GVYDWRAERE AVVGLEAVSD
SFSPMKVEKK SDGVTEIDDV LLIETQGETA QALAIRLARP VVVIDKMAGK VVTIAAAAVN
PDSATRKAIY YLQQQGKTVL QIADYPGMLI WRTVAMIINE ALDALQKGVA SEQDIDTAMR
LGVNYPYGPL AWGAQLGWQR ILRLLENLQH HYGEERYRPC SLLRQRALLE SGYES
