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Reviewed, UniProtKB/Swiss-Prot P49250 (AMO_KLEAE)

Last modified June 16, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Primary amine oxidase
    EC=1.4.3.21
Alternative name(s):
    Copper amine oxidase
    Monamine oxidase
    Tyramine oxidase
Gene names
Name: maoA
Synonyms: tynA
OrganismKlebsiella aerogenes
Taxonomic identifier28451 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length755 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Active on tyramine, tryptamine, beta-phenethylamine and dopamine.

Catalytic activity

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.

Cofactor

Binds 1 copper ion per subunit.

Contains 1 topaquinone per subunit By similarity.

Subcellular location

Periplasm.

Induction

By tyramine and catecholamines.

Post-translational modification

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

Sequence similarities

Belongs to the copper/topaquinone oxidase family.

Ontologies

Keywords
   Biological processCatecholamine metabolism
   Cellular componentPeriplasm
   DomainSignal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMTPQ
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcatecholamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionamine oxidase activity

Inferred from electronic annotation. Source: EC

copper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

quinone binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Ref.1
Chain31 – 755725Primary amine oxidase
PRO_0000035674

Sites

Active site4131Proton acceptor By similarity
Active site4961Schiff-base intermediate with substrate; via topaquinone By similarity
Metal binding5541Copper Potential
Metal binding5561Copper Potential
Metal binding7191Copper Potential

Amino acid modifications

Modified residue49612',4',5'-topaquinone By similarity

Sequences

Sequence LengthMass (Da)Tools
P49250-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 7B5552283CD93EFF

FASTA75583,577
        10         20         30         40         50         60 
MANGLKFSPR KTALALAVAV VCAWQSPVFA HGSEAHMVPL DKTLQEFGAD VQWDDYAQMF 

        70         80         90        100        110        120 
TLIKDGAYVK VKPGAKTAIV NGKSLDLPVP VVMKEGKAWV SDTFINDVFQ SGLDQTFQVE 

       130        140        150        160        170        180 
KRPHPLNSLS AAEISKAVTI VKAAPEFQPN TRFTEISLHE PDKAAVWAFA LQGTPVDAPR 

       190        200        210        220        230        240 
TADVVMLDGK HVIEAVVDLQ NKKILSWTPI KGAHGMVLLD DFVSVQNIIN TSSEFAEVLK 

       250        260        270        280        290        300 
KHGITDPGKV VTTPLTVGFF DGKDGLQQDA RLLKVVSYLD TGDGNYWAHP IENLVAVVDL 

       310        320        330        340        350        360 
EAKKIIKIEE GPVIPVPMEP RPYDGRDRNA PAVKPLEITE PEGKNYTITG DTIHWQNWDF 

       370        380        390        400        410        420 
HLRLNSRVGP ILSTVTYNDN GTKRQVMYEG SLGGMIVPYG DPDVGWYFKA YLDSGDYGMG 

       430        440        450        460        470        480 
TLTSPIVRGK DAPSNAVLLD ETIADYTGKP TTIPGAVAIF ERYAGPEYKH LEMGKPNVST 

       490        500        510        520        530        540 
ERRELVVRWI STVGNYDYIF DWVFHDNGTI GIDAGATGIE AVKGVLAKTM HDPSAKEDTR 

       550        560        570        580        590        600 
YGTLIDHNIV GTTHQHIYNF RLDLDVDGEN NTLVAMDPEV KPNTAGGPRT STMQVNQYTI 

       610        620        630        640        650        660 
DSEQKAAQKF DPGTIRLLSN TSKENRMGNP VSYQIIPYAG GTHPAATGAK FAPDEWIYHR 

       670        680        690        700        710        720 
LSFMDKQLWV TRYHPTERYP EGKYPNRSAH DTGLGQYAKD DESLTNHDDV VWITTGTTHV 

       730        740        750 
ARAEEWPIMP TEWALALLKP WNFFDETPTL GEKKK 

« Hide

References

[1]"A monoamine-regulated Klebsiella aerogenes operon containing the monoamine oxidase structural gene (maoA) and the maoC gene."
Sugino H., Sasaki M., Azakami H., Yamashita M., Murooka Y.
J. Bacteriol. 174:2485-2492(1992) [PubMed: 1556068] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-41.
Strain: W70.

Cross-references

Sequence databases

D10208 Genomic DNA. Translation: BAA01060.1.

3D structure databases

HSSPHSSP built from PDB template 1OAC based on UniProtKB P46883.
SMRP49250. Positions 35-754.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.4.3.6. 366.

Family and domain databases

InterProIPR000269. Cu_amine_oxidase.
IPR012854. Cu_amine_oxidase-like_N.
IPR015798. Cu_amine_oxidase_C.
IPR015800. Cu_amine_oxidase_N2.
IPR015801. Cu_amine_oxidase_N2/3.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
Gene3DG3DSA:3.30.457.10. Cu_amine_oxidase-like_N. 1 hit.
G3DSA:3.10.450.40. CuNH_oxidase. 2 hits.
G3DSA:2.70.98.20. Lyase_8_central. 1 hit.
PANTHERPTHR10638. CuNH_oxidase. 1 hit.
PfamPF01179. 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]
PROSITEPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMO_KLEAE
AccessionPrimary (citable) accession number: P49250
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents