Primary amine oxidase precursor - Klebsiella oxytoca (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC 1686)

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P80695 (AMO_KLEOK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 70. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Primary amine oxidase
EC=1.4.3.21

Alternative name(s):
Monamine oxidase
Tyramine oxidase

Gene names

Name:	maoA
Synonyms:	tynA
Ordered Locus Names:	KOX_19410

Organism

Klebsiella oxytoca (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC 1686) [Complete proteome] [HAMAP]

Taxonomic identifier

1006551 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella ›

Protein attributes

Sequence length	752 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Active on tyramine, tryptamine, beta-phenethylamine and dopamine. Ref.2
Catalytic activity	RCH₂NH₂ + H₂O + O₂ = RCHO + NH₃ + H₂O₂. Ref.2
Cofactor	Binds 1 copper ion per subunit. Ref.2 Contains 1 topaquinone per subunit By similarity. Ref.2
Subunit structure	Homodimer. Ref.2
Subcellular location	Periplasm Ref.2.
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 process	Catecholamine metabolism
Cellular component	Periplasm
Domain	Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	TPQ
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	amine metabolic process Inferred from electronic annotation. Source: InterPro catecholamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aliphatic-amine oxidase activity Inferred from electronic annotation. Source: EC aminoacetone:oxygen oxidoreductase(deaminating) activity Inferred from electronic annotation. Source: EC copper ion binding Inferred from electronic annotation. Source: InterPro phenethylamine:oxygen oxidoreductase (deaminating) activity Inferred from electronic annotation. Source: EC primary amine oxidase activity Inferred from electronic annotation. Source: EC quinone binding Inferred from electronic annotation. Source: InterPro tryptamine:oxygen oxidoreductase (deaminating) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

Ref.2

Chain

28 – 752

725

Primary amine oxidase

PRO_0000064108

Sequences

Sequence

Length

Mass (Da)

Tools

P80695 [UniParc].

Last modified May 16, 2012. Version 2.
Checksum: 956A1D24B3963A9C
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FASTA

752

83,624

        10         20         30         40         50         60 
MAILSPRKTA LALAVALSCA WQSPAFAHGG EAHMVPMDKT LQDFGADVQW DDYAQMFTLI 

        70         80         90        100        110        120 
KDGAYVKVKP GAKTAIVNGK TLELQVPVVM KDGKAWVSDT FINDVFQSGL DQTFQVEKRP 

       130        140        150        160        170        180 
HPLNSLSAAE ISAAVAIVKA AADFKPNTRF TEISLREPDK KAVWDFALNG TPVNAPRAAD 

       190        200        210        220        230        240 
VIMLDGKHVI EAVVDLQNKK VLSWTPIKDA HGMVLLDDFA SVQNIINASS EFAEVLKKHG 

       250        260        270        280        290        300 
IDDPSKVITT PLTVGYFDGK DGLKQDARLL KVVSYLDVGD GNYWAHPIEN LVAVVDLEQK 

       310        320        330        340        350        360 
KIIKIEEGPT IPVPMAARPY DGRDRVAPKI KPLDIIEPEG KNYTITGDMI HWQNWDFHLR 

       370        380        390        400        410        420 
MNSRVGPILS TVTYNDNGKK RQVMYEGSLG GMIVPYGDPD VGWYFKAYLD SGDYGMGTLT 

       430        440        450        460        470        480 
SPIVRGKDAP SNAVLLDETI ADYTGTPTTI PRAIAIFERY AGPEYKHQEM GKPNVSTERR 

       490        500        510        520        530        540 
ELVVRWISTV GNYDYIFDWV FHENGTIGID AGATGIEAVK GVQAKTMHDP SAKEDTRYGT 

       550        560        570        580        590        600 
LIDHNIVGTT HQHIYNFRLD LDVDGENNTL VAMDPEVKPN TAGGPRTSTM QINQYTIDSE 

       610        620        630        640        650        660 
QKAAQKFDPG TIRLLSNITK ENRMGNPVSY QIIPYAGGTH PVATGAKFAP DEWIYHRLSF 

       670        680        690        700        710        720 
MDKQLWVTRY HPTERFPEGK YPNRSIHDTG LGQYAKDDES LDNHDDVVWI TTGTTHVARA 

       730        740        750 
EEWPIMPTEW AHALLKPWNF FDETPTLGEK KE

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Klebsiella oxytoca strain KCTC 1686." Shin S.H., Kim S., Kim J.Y., Yang K.-S., Seo J.-S. Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC 1686.
[2]	"Distribution of amine oxidases and amine dehydrogenases in bacteria grown on primary amines and characterization of the amine oxidase from Klebsiella oxytoca." Hacisalihoglu A., Jongejan J.A., Duine J.A. Microbiology 143:505-512(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-47 AND 662-697, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. Strain: ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC 1686.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP003218 Genomic DNA. Translation: AEX05604.1.
RefSeq	YP_005019843.1. NC_016612.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AEX05604; AEX05604; KOX_19410.
GeneID	11661964.
KEGG	kox:KOX_19410.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K00276.
Enzyme and pathway databases
BRENDA	1.4.3.6. 2811.
Family and domain databases
Gene3D	2.70.98.20. 1 hit. 3.10.450.40. 2 hits. 3.30.457.10. 1 hit.
InterPro	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]
PANTHER	PTHR10638. PTHR10638. 1 hit.
Pfam	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]
SUPFAM	SSF55383. Cu_amine_oxidase-like_N. 1 hit. SSF54416. Cu_amine_oxidase_N-reg. 2 hits. SSF49998. CuNH_oxidase. 1 hit.
PROSITE	PS01164. COPPER_AMINE_OXID_1. 1 hit. PS01165. COPPER_AMINE_OXID_2. 1 hit. PS51257. PROKAR_LIPOPROTEIN. 1 hit. Uncertain. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMO_KLEOK

Accession

Primary (citable) accession number: P80695
Secondary accession number(s): G8WBD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 16, 2012
Last modified:	April 3, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents