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Protein

Bifunctional protein PaaZ

Gene

paaZ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolytic ring cleavage of 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA) via the open-chain aldehyde intermediate to yield 3-oxo-5,6-dehydrosuberyl-CoA. The enzyme consists of a C-terminal (R)-specific enoyl-CoA hydratase domain (formerly MaoC) that cleaves the ring and produces the highly reactive 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde and an N-terminal NADP-dependent aldehyde dehydrogenase domain that oxidizes the aldehyde to 3-oxo-5,6-dehydrosuberyl-CoA. Can also use crotonyl-CoA as substrate.3 Publications

Catalytic activityi

2-oxepin-2(3H)-ylideneacetyl-CoA + H2O = 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde.1 Publication
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + NADP+ + H2O = 3-oxo-5,6-dehydrosuberyl-CoA + NADPH.1 Publication

Kineticsi

  1. KM=11 µM for oxepin-CoA (at 22 degrees Celsius and pH 8)1 Publication
  2. KM=56 µM for NADP (at 22 degrees Celsius and pH 8)1 Publication

    pH dependencei

    Optimum pH is 8.1 Publication

    Pathwayi: phenylacetate degradation

    This protein is involved in the pathway phenylacetate degradation, which is part of Aromatic compound metabolism.
    View all proteins of this organism that are known to be involved in the pathway phenylacetate degradation and in Aromatic compound metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei256By similarity1
    Active sitei295By similarity1

    GO - Molecular functioni

    GO - Biological processi

    • phenylacetate catabolic process Source: UniProtKB

    Keywordsi

    Molecular functionHydrolase, Lyase, Multifunctional enzyme, Oxidoreductase
    LigandNADP

    Enzyme and pathway databases

    BioCyciEcoCyc:G6708-MONOMER
    MetaCyc:G6708-MONOMER
    BRENDAi3.3.2.12 2026
    UniPathwayiUPA00930

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional protein PaaZ
    Including the following 2 domains:
    2-oxepin-2(3H)-ylideneacetyl-CoA hydrolase (EC:3.3.2.12)
    Alternative name(s):
    Oxepin-CoA hydrolase
    3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (EC:1.2.1.911 Publication)
    Gene namesi
    Name:paaZ
    Synonyms:maoC, ydbN
    Ordered Locus Names:b1387, JW1382
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13735 paaZ

    Pathology & Biotechi

    Disruption phenotypei

    Disruption causes the conversion of phenylacetate (PA) into 2-hydroxyphenylacetate (2-HPA).1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi256E → Q: Catalyzes the formation of 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde instead of 3-oxo-5,6-dehydrosuberyl-CoA. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000565811 – 681Bifunctional protein PaaZAdd BLAST681

    Proteomic databases

    PaxDbiP77455
    PRIDEiP77455

    Expressioni

    Inductioni

    Activated by cAMP receptor protein (CRP) and integration host factor (IHF). Inhibited by PaaX.1 Publication

    Interactioni

    Protein-protein interaction databases

    BioGridi4260176, 262 interactors
    IntActiP77455, 3 interactors
    STRINGi316385.ECDH10B_1512

    Structurei

    3D structure databases

    ProteinModelPortaliP77455
    SMRiP77455
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini537 – 648MaoC-likeAdd BLAST112

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1 – 333Aldehyde dehydrogenaseAdd BLAST333

    Sequence similaritiesi

    In the N-terminal section; belongs to the aldehyde dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105DXM Bacteria
    COG2030 LUCA
    HOGENOMiHOG000249929
    InParanoidiP77455
    KOiK02618
    OMAiDTFYAHM
    PhylomeDBiP77455

    Family and domain databases

    Gene3Di3.40.309.10, 1 hit
    3.40.605.10, 2 hits
    InterProiView protein in InterPro
    IPR016161 Ald_DH/histidinol_DH
    IPR016163 Ald_DH_C
    IPR016162 Ald_DH_N
    IPR015590 Aldehyde_DH_dom
    IPR029069 HotDog_dom_sf
    IPR002539 MaoC_dom
    IPR011966 PaaN-DH
    PfamiView protein in Pfam
    PF00171 Aldedh, 1 hit
    PF01575 MaoC_dehydratas, 1 hit
    SUPFAMiSSF53720 SSF53720, 1 hit
    SSF54637 SSF54637, 1 hit
    TIGRFAMsiTIGR02278 PaaN-DH, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P77455-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQQLASFLSG TWQSGRGRSR LIHHAISGEA LWEVTSEGLD MAAARQFAIE
    60 70 80 90 100
    KGAPALRAMT FIERAAMLKA VAKHLLSEKE RFYALSAQTG ATRADSWVDI
    110 120 130 140 150
    EGGIGTLFTY ASLGSRELPD DTLWPEDELI PLSKEGGFAA RHLLTSKSGV
    160 170 180 190 200
    AVHINAFNFP CWGMLEKLAP TWLGGMPAII KPATATAQLT QAMVKSIVDS
    210 220 230 240 250
    GLVPEGAISL ICGSAGDLLD HLDSQDVVTF TGSAATGQML RVQPNIVAKS
    260 270 280 290 300
    IPFTMEADSL NCCVLGEDVT PDQPEFALFI REVVREMTTK AGQKCTAIRR
    310 320 330 340 350
    IIVPQALVNA VSDALVARLQ KVVVGDPAQE GVKMGALVNA EQRADVQEKV
    360 370 380 390 400
    NILLAAGCEI RLGGQADLSA AGAFFPPTLL YCPQPDETPA VHATEAFGPV
    410 420 430 440 450
    ATLMPAQNQR HALQLACAGG GSLAGTLVTA DPQIARQFIA DAARTHGRIQ
    460 470 480 490 500
    ILNEESAKES TGHGSPLPQL VHGGPGRAGG GEELGGLRAV KHYMQRTAVQ
    510 520 530 540 550
    GSPTMLAAIS KQWVRGAKVE EDRIHPFRKY FEELQPGDSL LTPRRTMTEA
    560 570 580 590 600
    DIVNFACLSG DHFYAHMDKI AAAESIFGER VVHGYFVLSA AAGLFVDAGV
    610 620 630 640 650
    GPVIANYGLE SLRFIEPVKP GDTIQVRLTC KRKTLKKQRS AEEKPTGVVE
    660 670 680
    WAVEVFNQHQ TPVALYSILT LVARQHGDFV D
    Length:681
    Mass (Da):73,003
    Last modified:February 1, 1997 - v1
    Checksum:iA631B97AA37A1C3E
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural varianti143L → V in strain: W. 1
    Natural varianti440A → T in strain: W. 1
    Natural varianti611S → N in strain: W. 1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X97452 Genomic DNA Translation: CAA66089.1
    U00096 Genomic DNA Translation: AAC74469.1
    AP009048 Genomic DNA Translation: BAA14997.1
    PIRiF64889
    RefSeqiNP_415905.1, NC_000913.3
    WP_001186469.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC74469; AAC74469; b1387
    BAA14997; BAA14997; BAA14997
    GeneIDi945954
    KEGGiecj:JW1382
    eco:b1387
    PATRICifig|1411691.4.peg.884

    Similar proteinsi

    Entry informationi

    Entry nameiPAAZ_ECOLI
    AccessioniPrimary (citable) accession number: P77455
    Secondary accession number(s): O53009
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: March 28, 2018
    This is version 134 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health