C2DQQ0 (C2DQQ0_ECOLX) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Adenosine deaminase HAMAP MF_00540
EC=3.5.4.4 HAMAP MF_00540

Alternative name(s):
Adenosine aminohydrolase HAMAP MF_00540

Gene names

Name:	add HAMAP MF_00540 EMBL EEJ47520.1
ORF Names:	HMPREF0358_2554 EMBL EEJ47520.1

Organism

Escherichia coli 83972 EMBL EEJ47520.1

Taxonomic identifier

525281 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Adenosine + H2O = inosine + NH3. HAMAP MF_00540
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00540 SAAS SAAS006330
Sequence similarities	Belongs to the adenosine and AMP deaminases family. Adenosine deaminase subfamily. HAMAP MF_00540

Ontologies

Keywords
Biological process	Nucleotide metabolism HAMAP MF_00540
Ligand	Metal-binding HAMAP MF_00540 SAAS SAAS006330 Zinc HAMAP MF_00540 SAAS SAAS006330
Molecular function	Hydrolase HAMAP MF_00540 SAAS SAAS006330 EMBL EEJ47520.1
Gene Ontology (GO)
Biological process	purine ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	adenosine deaminase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	200	1	Proton donor By similarity HAMAP MF_00540
	Metal binding	12	1	Zinc; catalytic By similarity HAMAP MF_00540
	Metal binding	14	1	Zinc; catalytic By similarity HAMAP MF_00540
	Metal binding	197	1	Zinc; catalytic By similarity HAMAP MF_00540
	Metal binding	278	1	Zinc; catalytic By similarity HAMAP MF_00540
	Binding site	14	1	Substrate By similarity HAMAP MF_00540
	Binding site	16	1	Substrate By similarity HAMAP MF_00540
	Binding site	170	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity HAMAP MF_00540
	Binding site	279	1	Substrate By similarity HAMAP MF_00540
	Site	221	1	Important for catalytic activity By similarity HAMAP MF_00540

Sequences

	Sequence		Length	Mass (Da)
	C2DQQ0 [UniParc]. Last modified June 16, 2009. Version 1. Checksum: A89FCBC00F5D3F47	FASTA	333	36,360
	10 20 30 40 50 60 MIDTTLPLTD IHRHLDGNIR PQTILELGRQ YNISLPAQSL ETLIPHVQVI ANEPDLVSFL 70 80 90 100 110 120 TKLDWGVKVL ASLDACRRVA FENIEDAARN GLHYVELRFS PGYMAMAHQL PVAGVVEAVI 130 140 150 160 170 180 DGVREGCRTF GVQAKLIGIM SRTFGEAACQ QELEAFLAHR DQITALDLAG DELGFPGSLF 190 200 210 220 230 240 LSHFNRARDA GWHITVHAGE AAGPESIWQA IRELGAERIG HGVKAIEDRA LMDFLAEQQI 250 260 270 280 290 300 GIESCLTSNI QTSTVADLAA HPLKTFLEHG IRASINTDDP GVQGVDIIHE YTVAAPAAGL 310 320 330 SREQIRQAQI NGLEMAFLSA EEKRALREKV AAK

References

[1]

Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y. , Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., Worley K., Gibbs R. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: 83972 EMBL EEJ47520.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	ACGN01000096 Genomic DNA. Translation: EEJ47520.1.
3D structure databases
ProteinModelPortal	C2DQQ0.
SMR	C2DQQ0. Positions 5-333.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
PATRIC	31217992. VBIEscCol21464_0884.
Family and domain databases
HAMAP	MF_00540. A_deaminase. [Tree]
InterPro	IPR006650. A/AMP_deam_AS. IPR001365. A/AMP_deaminase_dom. IPR006330. A_deaminase. [Graphical view]
Pfam	PF00962. A_deaminase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01430. Aden_deam. 1 hit.
PROSITE	PS00485. A_DEAMINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C2DQQ0_ECOLX

Accession

Primary (citable) accession number: C2DQQ0

Entry history

Integrated into UniProtKB/TrEMBL:	June 16, 2009
Last sequence update:	June 16, 2009
Last modified:	December 14, 2011
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)