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P46883

- AMO_ECOLI

UniProt

P46883 - AMO_ECOLI

Protein

Primary amine oxidase

Gene

tynA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    The enzyme prefers aromatic over aliphatic amines.

    Catalytic activityi

    RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.
    2-phenylethylamine + H2O + O2 = phenylacetaldehyde + NH3 + H2O2.

    Cofactori

    Binds 1 copper ion per subunit.
    Binds 2 calcium ions per subunit.
    Contains 1 topaquinone per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei413 – 4131Proton acceptorCurated
    Active sitei496 – 4961Schiff-base intermediate with substrate; via topaquinone
    Metal bindingi554 – 5541Copper
    Metal bindingi556 – 5561Copper
    Metal bindingi563 – 5631Calcium 1
    Metal bindingi564 – 5641Calcium 1; via carbonyl oxygen
    Metal bindingi565 – 5651Calcium 1
    Metal bindingi603 – 6031Calcium 2
    Metal bindingi700 – 7001Calcium 2
    Metal bindingi702 – 7021Calcium 2
    Metal bindingi708 – 7081Calcium 1
    Metal bindingi709 – 7091Calcium 1; via carbonyl oxygen
    Metal bindingi709 – 7091Calcium 2; via carbonyl oxygen
    Metal bindingi719 – 7191Copper

    GO - Molecular functioni

    1. aliphatic-amine oxidase activity Source: UniProtKB-EC
    2. aminoacetone:oxygen oxidoreductase(deaminating) activity Source: UniProtKB-EC
    3. calcium ion binding Source: EcoCyc
    4. copper ion binding Source: EcoCyc
    5. phenethylamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC
    6. primary amine oxidase activity Source: EcoCyc
    7. quinone binding Source: EcoCyc
    8. tryptamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC

    GO - Biological processi

    1. L-phenylalanine catabolic process Source: UniProtKB-UniPathway
    2. oxidation-reduction process Source: EcoCyc
    3. phenylethylamine catabolic process Source: EcoCyc

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Calcium, Copper, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:AMINEOXID-MONOMER.
    ECOL316407:JW1381-MONOMER.
    MetaCyc:AMINEOXID-MONOMER.
    UniPathwayiUPA00139; UER00723.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Primary amine oxidase (EC:1.4.3.21)
    Alternative name(s):
    2-phenylethylamine oxidase
    Copper amine oxidase
    Tyramine oxidase
    Gene namesi
    Name:tynA
    Synonyms:maoA
    Ordered Locus Names:b1386, JW1381
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG13140. tynA.

    Subcellular locationi

    GO - Cellular componenti

    1. periplasmic space Source: EcoCyc

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 30303 PublicationsAdd
    BLAST
    Chaini31 – 757727Primary amine oxidasePRO_0000035673Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei496 – 49612',4',5'-topaquinone

    Post-translational modificationi

    Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.

    Keywords - PTMi

    TPQ

    Proteomic databases

    PaxDbiP46883.
    PRIDEiP46883.

    Expressioni

    Gene expression databases

    GenevestigatoriP46883.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    DIPiDIP-11057N.
    IntActiP46883. 6 interactions.
    STRINGi511145.b1386.

    Structurei

    Secondary structure

    1
    757
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi37 – 393
    Helixi40 – 467
    Beta strandi50 – 545
    Turni55 – 584
    Beta strandi59 – 646
    Beta strandi67 – 715
    Beta strandi76 – 805
    Beta strandi83 – 864
    Beta strandi92 – 965
    Beta strandi98 – 1003
    Helixi104 – 1096
    Beta strandi110 – 1123
    Beta strandi116 – 1183
    Helixi131 – 14212
    Beta strandi152 – 1598
    Helixi163 – 17210
    Beta strandi181 – 1888
    Beta strandi191 – 1988
    Turni199 – 2024
    Beta strandi203 – 2108
    Helixi219 – 23012
    Helixi233 – 2419
    Helixi247 – 2493
    Beta strandi250 – 2556
    Turni261 – 2644
    Beta strandi268 – 2703
    Beta strandi272 – 2798
    Beta strandi282 – 2843
    Helixi286 – 2883
    Beta strandi294 – 2996
    Turni300 – 3034
    Beta strandi304 – 3107
    Beta strandi323 – 3253
    Beta strandi337 – 3393
    Beta strandi345 – 3495
    Beta strandi352 – 3554
    Beta strandi358 – 3658
    Turni366 – 3683
    Beta strandi369 – 37911
    Beta strandi382 – 39918
    Turni404 – 4085
    Beta strandi410 – 4123
    Helixi413 – 4175
    Turni419 – 4224
    Turni428 – 4303
    Beta strandi437 – 4448
    Beta strandi450 – 47021
    Beta strandi478 – 49316
    Beta strandi496 – 50510
    Beta strandi510 – 5189
    Beta strandi522 – 5243
    Helixi535 – 5384
    Turni539 – 5413
    Beta strandi542 – 5465
    Beta strandi549 – 5524
    Beta strandi554 – 56411
    Beta strandi568 – 58215
    Beta strandi590 – 60011
    Helixi603 – 6064
    Beta strandi614 – 62411
    Beta strandi630 – 64314
    Helixi656 – 6605
    Helixi662 – 6654
    Beta strandi667 – 6726
    Helixi694 – 6974
    Turni698 – 7003
    Beta strandi707 – 71913
    Helixi723 – 7253
    Beta strandi726 – 74621

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D6UX-ray2.40A/B31-757[»]
    1D6YX-ray2.40A/B31-757[»]
    1D6ZX-ray2.10A/B31-757[»]
    1DYUX-ray2.04A/B31-757[»]
    1JRQX-ray2.15A/B31-757[»]
    1LVNX-ray2.40A/B31-757[»]
    1OACX-ray2.00A/B31-757[»]
    1QAFX-ray2.20A/B36-756[»]
    1QAKX-ray2.00A/B36-757[»]
    1QALX-ray2.20A/B36-756[»]
    1SPUX-ray2.00A/B31-757[»]
    2W0QX-ray2.48A/B31-757[»]
    2WGQX-ray2.50A/B31-757[»]
    2WO0X-ray2.60A/B31-757[»]
    2WOFX-ray2.25A/B31-757[»]
    2WOHX-ray2.70A/B31-757[»]
    ProteinModelPortaliP46883.
    SMRiP46883. Positions 35-757.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46883.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the copper/topaquinone oxidase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3733.
    HOGENOMiHOG000250947.
    KOiK00276.
    OMAiIENTFHP.
    OrthoDBiEOG6FFS27.
    PhylomeDBiP46883.

    Family and domain databases

    Gene3Di2.70.98.20. 1 hit.
    3.10.450.40. 2 hits.
    3.30.457.10. 1 hit.
    InterProiIPR000269. Cu_amine_oxidase.
    IPR012854. Cu_amine_oxidase-like_N.
    IPR015798. Cu_amine_oxidase_C.
    IPR016182. Cu_amine_oxidase_N-reg.
    IPR015800. Cu_amine_oxidase_N2.
    IPR015801. Cu_amine_oxidase_N2/3.
    IPR015802. Cu_amine_oxidase_N3.
    [Graphical view]
    PANTHERiPTHR10638. PTHR10638. 1 hit.
    PfamiPF01179. Cu_amine_oxid. 1 hit.
    PF07833. Cu_amine_oxidN1. 1 hit.
    PF02727. Cu_amine_oxidN2. 1 hit.
    PF02728. Cu_amine_oxidN3. 1 hit.
    [Graphical view]
    SUPFAMiSSF49998. SSF49998. 1 hit.
    SSF54416. SSF54416. 2 hits.
    SSF55383. SSF55383. 1 hit.
    PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
    PS01165. COPPER_AMINE_OXID_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P46883-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSPSLYSAR KTTLALAVAL SFAWQAPVFA HGGEAHMVPM DKTLKEFGAD    50
    VQWDDYAQLF TLIKDGAYVK VKPGAQTAIV NGQPLALQVP VVMKDNKAWV 100
    SDTFINDVFQ SGLDQTFQVE KRPHPLNALT ADEIKQAVEI VKASADFKPN 150
    TRFTEISLLP PDKEAVWAFA LENKPVDQPR KADVIMLDGK HIIEAVVDLQ 200
    NNKLLSWQPI KDAHGMVLLD DFASVQNIIN NSEEFAAAVK KRGITDAKKV 250
    ITTPLTVGYF DGKDGLKQDA RLLKVISYLD VGDGNYWAHP IENLVAVVDL 300
    EQKKIVKIEE GPVVPVPMTA RPFDGRDRVA PAVKPMQIIE PEGKNYTITG 350
    DMIHWRNWDF HLSMNSRVGP MISTVTYNDN GTKRKVMYEG SLGGMIVPYG 400
    DPDIGWYFKA YLDSGDYGMG TLTSPIARGK DAPSNAVLLN ETIADYTGVP 450
    MEIPRAIAVF ERYAGPEYKH QEMGQPNVST ERRELVVRWI STVGNYDYIF 500
    DWIFHENGTI GIDAGATGIE AVKGVKAKTM HDETAKDDTR YGTLIDHNIV 550
    GTTHQHIYNF RLDLDVDGEN NSLVAMDPVV KPNTAGGPRT STMQVNQYNI 600
    GNEQDAAQKF DPGTIRLLSN PNKENRMGNP VSYQIIPYAG GTHPVAKGAQ 650
    FAPDEWIYHR LSFMDKQLWV TRYHPGERFP EGKYPNRSTH DTGLGQYSKD 700
    NESLDNTDAV VWMTTGTTHV ARAEEWPIMP TEWVHTLLKP WNFFDETPTL 750
    GALKKDK 757
    Length:757
    Mass (Da):84,379
    Last modified:November 1, 1995 - v1
    Checksum:i65600BCED35243DB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331G → E AA sequence (PubMed:8631685)Curated
    Sequence conflicti248 – 2481K → E in BAA04900. 1 PublicationCurated
    Sequence conflicti258 – 2592GY → VI in BAA04900. 1 PublicationCurated
    Sequence conflicti276 – 2761I → II in BAA04900. 1 PublicationCurated
    Sequence conflicti288 – 2881Missing1 PublicationCurated
    Sequence conflicti290 – 2901P → I1 PublicationCurated
    Sequence conflicti456 – 4561A → P in BAA04900. 1 PublicationCurated
    Sequence conflicti659 – 6591H → D in BAA04900. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti42 – 421K → E in strain: W.
    Natural varianti59 – 591L → I in strain: W.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D23670 Genomic DNA. Translation: BAA04900.1.
    L47571 Genomic DNA. Translation: AAC37012.1.
    U00096 Genomic DNA. Translation: AAC74468.1.
    AP009048 Genomic DNA. Translation: BAA14996.1.
    X97452 Genomic DNA. Translation: CAA66104.1.
    X97453 Genomic DNA. Translation: CAA66107.1.
    PIRiE64889.
    RefSeqiNP_415904.3. NC_000913.3.
    YP_489655.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74468; AAC74468; b1386.
    BAA14996; BAA14996; BAA14996.
    GeneIDi12931183.
    945939.
    KEGGiecj:Y75_p1363.
    eco:b1386.
    PATRICi32118058. VBIEscCol129921_1449.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D23670 Genomic DNA. Translation: BAA04900.1 .
    L47571 Genomic DNA. Translation: AAC37012.1 .
    U00096 Genomic DNA. Translation: AAC74468.1 .
    AP009048 Genomic DNA. Translation: BAA14996.1 .
    X97452 Genomic DNA. Translation: CAA66104.1 .
    X97453 Genomic DNA. Translation: CAA66107.1 .
    PIRi E64889.
    RefSeqi NP_415904.3. NC_000913.3.
    YP_489655.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D6U X-ray 2.40 A/B 31-757 [» ]
    1D6Y X-ray 2.40 A/B 31-757 [» ]
    1D6Z X-ray 2.10 A/B 31-757 [» ]
    1DYU X-ray 2.04 A/B 31-757 [» ]
    1JRQ X-ray 2.15 A/B 31-757 [» ]
    1LVN X-ray 2.40 A/B 31-757 [» ]
    1OAC X-ray 2.00 A/B 31-757 [» ]
    1QAF X-ray 2.20 A/B 36-756 [» ]
    1QAK X-ray 2.00 A/B 36-757 [» ]
    1QAL X-ray 2.20 A/B 36-756 [» ]
    1SPU X-ray 2.00 A/B 31-757 [» ]
    2W0Q X-ray 2.48 A/B 31-757 [» ]
    2WGQ X-ray 2.50 A/B 31-757 [» ]
    2WO0 X-ray 2.60 A/B 31-757 [» ]
    2WOF X-ray 2.25 A/B 31-757 [» ]
    2WOH X-ray 2.70 A/B 31-757 [» ]
    ProteinModelPortali P46883.
    SMRi P46883. Positions 35-757.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-11057N.
    IntActi P46883. 6 interactions.
    STRINGi 511145.b1386.

    Proteomic databases

    PaxDbi P46883.
    PRIDEi P46883.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74468 ; AAC74468 ; b1386 .
    BAA14996 ; BAA14996 ; BAA14996 .
    GeneIDi 12931183.
    945939.
    KEGGi ecj:Y75_p1363.
    eco:b1386.
    PATRICi 32118058. VBIEscCol129921_1449.

    Organism-specific databases

    EchoBASEi EB2934.
    EcoGenei EG13140. tynA.

    Phylogenomic databases

    eggNOGi COG3733.
    HOGENOMi HOG000250947.
    KOi K00276.
    OMAi IENTFHP.
    OrthoDBi EOG6FFS27.
    PhylomeDBi P46883.

    Enzyme and pathway databases

    UniPathwayi UPA00139 ; UER00723 .
    BioCyci EcoCyc:AMINEOXID-MONOMER.
    ECOL316407:JW1381-MONOMER.
    MetaCyc:AMINEOXID-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P46883.
    PROi P46883.

    Gene expression databases

    Genevestigatori P46883.

    Family and domain databases

    Gene3Di 2.70.98.20. 1 hit.
    3.10.450.40. 2 hits.
    3.30.457.10. 1 hit.
    InterProi IPR000269. Cu_amine_oxidase.
    IPR012854. Cu_amine_oxidase-like_N.
    IPR015798. Cu_amine_oxidase_C.
    IPR016182. Cu_amine_oxidase_N-reg.
    IPR015800. Cu_amine_oxidase_N2.
    IPR015801. Cu_amine_oxidase_N2/3.
    IPR015802. Cu_amine_oxidase_N3.
    [Graphical view ]
    PANTHERi PTHR10638. PTHR10638. 1 hit.
    Pfami PF01179. Cu_amine_oxid. 1 hit.
    PF07833. Cu_amine_oxidN1. 1 hit.
    PF02727. Cu_amine_oxidN2. 1 hit.
    PF02728. Cu_amine_oxidN3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49998. SSF49998. 1 hit.
    SSF54416. SSF54416. 2 hits.
    SSF55383. SSF55383. 1 hit.
    PROSITEi PS01164. COPPER_AMINE_OXID_1. 1 hit.
    PS01165. COPPER_AMINE_OXID_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the gene for monoamine oxidase (maoA) from Escherichia coli."
      Azakami H., Yamashita M., Roh J.-H., Suzuki H., Kumagai H., Murooka Y.
      J. Ferment. Bioeng. 77:315-319(1994)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. "Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2-A resolution."
      Parsons M.R., Convery M.A., Wilmot C.M., Yadav K.D.S., Blakeley V., Corner A.S., Phillips S.E.V., McPherson M.J., Knowles P.F.
      Structure 3:1171-1184(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
      Strain: K12 / K10.
    3. "Cloning of the maoA gene that encodes aromatic amine oxidase of Escherichia coli W3350 and characterization of the overexpressed enzyme."
      Steinebach V., Benen J.A.E., Bader R., Postma P.W., De Vries S., Duine J.A.
      Eur. J. Biochem. 237:584-591(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-35, CHARACTERIZATION.
      Strain: K12 / W3350 / ATCC 27020.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway."
      Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M., Garcia J.L., Diaz E.
      J. Biol. Chem. 273:25974-25986(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
      Strain: W / ATCC 11105 / DSM 1900.
    8. "Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli."
      Ferrandez A., Prieto M.A., Garcia J.L., Diaz E.
      FEBS Lett. 406:23-27(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 477-757.
      Strain: W / ATCC 11105 / DSM 1900.
    9. "maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli."
      Yamashita M., Azakami H., Yokoro N., Roh J.-H., Suzuki H., Kumagai H., Murooka Y.
      J. Bacteriol. 178:2941-2947(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 31-50.
    10. "2-phenylethylamine catabolism by Escherichia coli K-12: gene organization and expression."
      Hanlon S.P., Hill T.K., Flavell M.A., Stringfellow J.M., Cooper R.A.
      Microbiology 143:513-518(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 31-40.
      Strain: K12.
    11. "Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction."
      Wilmot C.M., Murray J.M., Alton G., Parsons M.R., Convery M.A., Blakeley V., Corner A.S., Palcic M.M., Knowles P.F., McPherson M.J., Phillips S.E.V.
      Biochemistry 36:1608-1620(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    12. "The active site base controls cofactor reactivity in Escherichia coli amine oxidase: X-ray crystallographic studies with mutational variants."
      Murray J.M., Saysell C.G., Wilmot C.M., Tambyrajah W.S., Jaeger J., Knowles P.F., Phillips S.E.V., McPherson M.J.
      Biochemistry 38:8217-8227(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    13. "Visualization of dioxygen bound to copper during enzyme catalysis."
      Wilmot C.M., Hajdu J., McPherson M.J., Knowles P.F., Phillips S.E.
      Science 286:1724-1728(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

    Entry informationi

    Entry nameiAMO_ECOLI
    AccessioniPrimary (citable) accession number: P46883
    Secondary accession number(s): O53008, P78153
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 146 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    When highly overexpressed there can be substoichiometric amounts of TPQ in the enzyme; this may be due to imperfect conversion of tyrosine to TPQ (see PubMed:8647101).Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3