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P46883

- AMO_ECOLI

UniProt

P46883 - AMO_ECOLI

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Protein

Primary amine oxidase

Gene

tynA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

The enzyme prefers aromatic over aliphatic amines.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Cu cationNote: Binds 1 copper ion per subunit.
  • Ca2+Note: Binds 2 calcium ions per subunit.
  • L-topaquinoneNote: 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
Complete GO annotation...

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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP46883.
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

        10         20         30         40         50
MGSPSLYSAR KTTLALAVAL SFAWQAPVFA HGGEAHMVPM DKTLKEFGAD
60 70 80 90 100
VQWDDYAQLF TLIKDGAYVK VKPGAQTAIV NGQPLALQVP VVMKDNKAWV
110 120 130 140 150
SDTFINDVFQ SGLDQTFQVE KRPHPLNALT ADEIKQAVEI VKASADFKPN
160 170 180 190 200
TRFTEISLLP PDKEAVWAFA LENKPVDQPR KADVIMLDGK HIIEAVVDLQ
210 220 230 240 250
NNKLLSWQPI KDAHGMVLLD DFASVQNIIN NSEEFAAAVK KRGITDAKKV
260 270 280 290 300
ITTPLTVGYF DGKDGLKQDA RLLKVISYLD VGDGNYWAHP IENLVAVVDL
310 320 330 340 350
EQKKIVKIEE GPVVPVPMTA RPFDGRDRVA PAVKPMQIIE PEGKNYTITG
360 370 380 390 400
DMIHWRNWDF HLSMNSRVGP MISTVTYNDN GTKRKVMYEG SLGGMIVPYG
410 420 430 440 450
DPDIGWYFKA YLDSGDYGMG TLTSPIARGK DAPSNAVLLN ETIADYTGVP
460 470 480 490 500
MEIPRAIAVF ERYAGPEYKH QEMGQPNVST ERRELVVRWI STVGNYDYIF
510 520 530 540 550
DWIFHENGTI GIDAGATGIE AVKGVKAKTM HDETAKDDTR YGTLIDHNIV
560 570 580 590 600
GTTHQHIYNF RLDLDVDGEN NSLVAMDPVV KPNTAGGPRT STMQVNQYNI
610 620 630 640 650
GNEQDAAQKF DPGTIRLLSN PNKENRMGNP VSYQIIPYAG GTHPVAKGAQ
660 670 680 690 700
FAPDEWIYHR LSFMDKQLWV TRYHPGERFP EGKYPNRSTH DTGLGQYSKD
710 720 730 740 750
NESLDNTDAV VWMTTGTTHV ARAEEWPIMP TEWVHTLLKP WNFFDETPTL

GALKKDK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P46883.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 148 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