PAAZ_ECOLI
ID PAAZ_ECOLI Reviewed; 681 AA.
AC P77455; O53009;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Bifunctional protein PaaZ;
DE Includes:
DE RecName: Full=2-oxepin-2(3H)-ylideneacetyl-CoA hydrolase;
DE EC=3.3.2.12;
DE AltName: Full=Oxepin-CoA hydrolase;
DE Includes:
DE RecName: Full=3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase;
DE EC=1.2.1.91 {ECO:0000269|PubMed:21296885};
GN Name=paaZ; Synonyms=maoC, ydbN; OrderedLocusNames=b1387, JW1382;
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 DISRUPTION PHENOTYPE.
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 FUNCTION AS A HYDROLASE AND SEMIALDEHYDE DEHYDROGENASE.
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 [7]
RP FUNCTION AS A HYDROLASE AND SEMIALDEHYDE DEHYDROGENASE, REACTION MECHANISM,
RP MUTAGENESIS OF GLU-256, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND SUBSTRATE SPECIFICITY.
RX PubMed=21296885; DOI=10.1074/jbc.m110.196667;
RA Teufel R., Gantert C., Voss M., Eisenreich W., Haehnel W., Fuchs G.;
RT "Studies on the mechanism of ring hydrolysis in phenylacetate degradation:
RT a metabolic branching point.";
RL J. Biol. Chem. 286:11021-11034(2011).
CC -!- FUNCTION: Catalyzes the hydrolytic ring cleavage of 2-oxepin-2(3H)-
CC ylideneacetyl-CoA (oxepin-CoA) via the open-chain aldehyde intermediate
CC to yield 3-oxo-5,6-dehydrosuberyl-CoA. The enzyme consists of a C-
CC terminal (R)-specific enoyl-CoA hydratase domain (formerly MaoC) that
CC cleaves the ring and produces the highly reactive 3-oxo-5,6-
CC dehydrosuberyl-CoA semialdehyde and an N-terminal NADP-dependent
CC aldehyde dehydrogenase domain that oxidizes the aldehyde to 3-oxo-5,6-
CC dehydrosuberyl-CoA. Can also use crotonyl-CoA as substrate.
CC {ECO:0000269|PubMed:20660314, ECO:0000269|PubMed:21296885,
CC ECO:0000269|PubMed:9748275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxepin-2(3H)-ylideneacetyl-CoA + H2O = 3-oxo-5,6-
CC dehydrosuberyl-CoA semialdehyde; Xref=Rhea:RHEA:31755,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:63252, ChEBI:CHEBI:63257; EC=3.3.2.12;
CC Evidence={ECO:0000269|PubMed:21296885};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + H2O + NADP(+) = 3-
CC oxo-5,6-didehydrosuberyl-CoA + 2 H(+) + NADPH; Xref=Rhea:RHEA:31747,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:63255, ChEBI:CHEBI:63257; EC=1.2.1.91;
CC Evidence={ECO:0000269|PubMed:21296885};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for oxepin-CoA (at 22 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:21296885};
CC KM=56 uM for NADP (at 22 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:21296885};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:21296885};
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC -!- INDUCTION: Activated by cAMP receptor protein (CRP) and integration
CC host factor (IHF). Inhibited by PaaX. {ECO:0000269|PubMed:10766858}.
CC -!- DISRUPTION PHENOTYPE: Disruption causes the conversion of phenylacetate
CC (PA) into 2-hydroxyphenylacetate (2-HPA). {ECO:0000269|PubMed:9748275}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aldehyde
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; X97452; CAA66089.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74469.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14997.1; -; Genomic_DNA.
DR PIR; F64889; F64889.
DR RefSeq; NP_415905.1; NC_000913.3.
DR RefSeq; WP_001186469.1; NZ_LN832404.1.
DR PDB; 6JQL; EM; 2.90 A; A/B/C/D/E/F=2-681.
DR PDB; 6JQM; EM; 3.30 A; A/B/C/D/E/F=2-681.
DR PDB; 6JQN; EM; 3.10 A; A/B/C/D/E/F=2-681.
DR PDB; 6JQO; EM; 3.10 A; A/B/C/D/E/F=2-681.
DR PDBsum; 6JQL; -.
DR PDBsum; 6JQM; -.
DR PDBsum; 6JQN; -.
DR PDBsum; 6JQO; -.
DR AlphaFoldDB; P77455; -.
DR SASBDB; P77455; -.
DR SMR; P77455; -.
DR BioGRID; 4260176; 262.
DR IntAct; P77455; 3.
DR STRING; 511145.b1387; -.
DR PaxDb; P77455; -.
DR PRIDE; P77455; -.
DR EnsemblBacteria; AAC74469; AAC74469; b1387.
DR EnsemblBacteria; BAA14997; BAA14997; BAA14997.
DR GeneID; 945954; -.
DR KEGG; ecj:JW1382; -.
DR KEGG; eco:b1387; -.
DR PATRIC; fig|1411691.4.peg.884; -.
DR EchoBASE; EB3498; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG2030; Bacteria.
DR HOGENOM; CLU_025047_0_0_6; -.
DR InParanoid; P77455; -.
DR OMA; DTFYAHM; -.
DR PhylomeDB; P77455; -.
DR BioCyc; EcoCyc:G6708-MON; -.
DR BioCyc; MetaCyc:G6708-MON; -.
DR BRENDA; 3.3.2.12; 2026.
DR UniPathway; UPA00930; -.
DR PRO; PR:P77455; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:EcoCyc.
DR GO; GO:0016803; F:ether hydrolase activity; IDA:EcoCyc.
DR GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0010124; P:phenylacetate catabolic process; IMP:UniProtKB.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR011966; PaaN-DH.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR02278; PaaN-DH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Lyase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..681
FT /note="Bifunctional protein PaaZ"
FT /id="PRO_0000056581"
FT DOMAIN 537..648
FT /note="MaoC-like"
FT REGION 1..333
FT /note="Aldehyde dehydrogenase"
FT REGION 456..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 256
FT /evidence="ECO:0000250"
FT ACT_SITE 295
FT /evidence="ECO:0000250"
FT VARIANT 143
FT /note="L -> V (in strain: W)"
FT VARIANT 440
FT /note="A -> T (in strain: W)"
FT VARIANT 611
FT /note="S -> N (in strain: W)"
FT MUTAGEN 256
FT /note="E->Q: Catalyzes the formation of 3-oxo-5,6-
FT dehydrosuberyl-CoA semialdehyde instead of 3-oxo-5,6-
FT dehydrosuberyl-CoA."
FT /evidence="ECO:0000269|PubMed:21296885"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:6JQL"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 93..116
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:6JQL"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:6JQN"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:6JQL"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:6JQN"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:6JQL"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 274..288
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 308..319
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 340..353
FT /evidence="ECO:0007829|PDB:6JQL"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:6JQL"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:6JQN"
FT TURN 389..393
FT /evidence="ECO:0007829|PDB:6JQL"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 400..407
FT /evidence="ECO:0007829|PDB:6JQL"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 432..442
FT /evidence="ECO:0007829|PDB:6JQL"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:6JQL"
FT TURN 454..457
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:6JQN"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 486..493
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 494..501
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 503..510
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:6JQN"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 549..559
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 569..573
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 575..579
FT /evidence="ECO:0007829|PDB:6JQL"
FT HELIX 584..595
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 622..632
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 639..643
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 646..656
FT /evidence="ECO:0007829|PDB:6JQL"
FT STRAND 664..673
FT /evidence="ECO:0007829|PDB:6JQL"
SQ SEQUENCE 681 AA; 73003 MW; A631B97AA37A1C3E CRC64;
MQQLASFLSG TWQSGRGRSR LIHHAISGEA LWEVTSEGLD MAAARQFAIE KGAPALRAMT
FIERAAMLKA VAKHLLSEKE RFYALSAQTG ATRADSWVDI EGGIGTLFTY ASLGSRELPD
DTLWPEDELI PLSKEGGFAA RHLLTSKSGV AVHINAFNFP CWGMLEKLAP TWLGGMPAII
KPATATAQLT QAMVKSIVDS GLVPEGAISL ICGSAGDLLD HLDSQDVVTF TGSAATGQML
RVQPNIVAKS IPFTMEADSL NCCVLGEDVT PDQPEFALFI REVVREMTTK AGQKCTAIRR
IIVPQALVNA VSDALVARLQ KVVVGDPAQE GVKMGALVNA EQRADVQEKV NILLAAGCEI
RLGGQADLSA AGAFFPPTLL YCPQPDETPA VHATEAFGPV ATLMPAQNQR HALQLACAGG
GSLAGTLVTA DPQIARQFIA DAARTHGRIQ ILNEESAKES TGHGSPLPQL VHGGPGRAGG
GEELGGLRAV KHYMQRTAVQ GSPTMLAAIS KQWVRGAKVE EDRIHPFRKY FEELQPGDSL
LTPRRTMTEA DIVNFACLSG DHFYAHMDKI AAAESIFGER VVHGYFVLSA AAGLFVDAGV
GPVIANYGLE SLRFIEPVKP GDTIQVRLTC KRKTLKKQRS AEEKPTGVVE WAVEVFNQHQ
TPVALYSILT LVARQHGDFV D
