B7L6A6 (B7L6A6_ECO55) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Amine oxidase RuleBase RU000672

Gene names

Name:	tynA EMBL CAU97379.1
Ordered Locus Names:	EC55989_1522 EMBL CAU97379.1

Organism

Escherichia coli (strain 55989 / EAEC) [Complete proteome] [HAMAP] EMBL CAU97379.1

Taxonomic identifier

585055 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	757 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Post-translational modification	Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue By similarity. RuleBase RU000672
Sequence similarities	Belongs to the copper/topaquinone oxidase family. RuleBase RU004199

Ontologies

Keywords
Ligand	Copper RuleBase RU000672 Metal-binding RuleBase RU000672
Molecular function	Oxidoreductase RuleBase RU000672 EMBL CAU97379.1
PTM	TPQ RuleBase RU000672
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	amine metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro primary amine oxidase activity Inferred from electronic annotation. Source: InterPro quinone binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	B7L6A6 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: DE5B57E65837A887	FASTA	757	84,384
	10 20 30 40 50 60 MGSPSLYSAR KTTLALAVAL SFAWQAPVFA HGGEAHMVPM DETLKEFGAD VQWDDYAQIF 70 80 90 100 110 120 TLIKDGAYVK VKPGAQTAIV NGQPLALQVP VVMKDNKAWV SDTFINDVFQ SGLDQTFQVE 130 140 150 160 170 180 KRPHPLNALT ADEIKQAVEI VKASADFKPN TRFTEISLLP PDKEAVWAFA LENKPVDQPR 190 200 210 220 230 240 KADVIMLDGK HIIEAVVDLQ NNKLLSWQPI KDAHGMVLLD DFASVQNIIN NSEEFAAAVK 250 260 270 280 290 300 KRGITDAKKV ITTPLTVGYF DGKDGLKQDA RLLKVISYLD VGDGNYWAHP IENLVAVVDL 310 320 330 340 350 360 EQKKIVKIEE GAVVPVPMTA RPFDGRDRVA PAVKPMQIIE PEGKNYTITG DMIHWRNWDF 370 380 390 400 410 420 HLSMNSRVGP MISTVTYNDN GTKRKVMYEG SLGGMIVPYG DPDIGWYFKA YLDSGDYGMG 430 440 450 460 470 480 TLTSPIARGK DAPSNAVLLN ETIADYTGVP MEIPRAIAVF ERYAGPEYKH QEMGQPNVST 490 500 510 520 530 540 ERRELVVRWI STVGNYDYIF DWIFHENGTI GIDAGATGIE AVKGVKAKTM HDETAKDDTR 550 560 570 580 590 600 YGTLIDHNIV GTTHQHIYNF RLDLDVDGEN NSLVAMDPVV KPNTAGGPRT STMQVNQYNI 610 620 630 640 650 660 GNEQDAAQKF DPGTIRLLSN LNKENRMGNP VSYQIIPYAG GTHPVAKGAQ FAPDEWIYHR 670 680 690 700 710 720 LSFMDKQLWV TRYHPGERFP EGKYPNRSTH DTGLGQYSKD NESLDNTDAV IWMTTGTTHV 730 740 750 ARAEEWPIMP TEWVHTLLKP WNFFDETPTL GALKKDK

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 55989 / EAEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928145 Genomic DNA. Translation: CAU97379.1.
RefSeq	YP_002402599.1. NC_011748.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	585055.EC55989_1522.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAU97379; CAU97379; EC55989_1522.
GeneID	7146077.
KEGG	eck:EC55989_1522.
PATRIC	38476492. VBIEscCol113220_1553.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3733.
HOGENOM	HOG000250947.
KO	K00276.
OMA	TSKENRM.
ProtClustDB	PRK14696.
Enzyme and pathway databases
BioCyc	ECOL585055:GJOM-1556-MONOMER.
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. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

B7L6A6_ECO55

Accession

Primary (citable) accession number: B7L6A6

Entry history

Integrated into UniProtKB/TrEMBL:	February 10, 2009
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)