Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Adenosine deaminase

Gene

Bamb_4621

Organism
Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

Zn2+SAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Zinc; via tele nitrogenCombined sources
Metal bindingi36 – 361Zinc; via tele nitrogenCombined sources
Metal bindingi215 – 2151Zinc; via tele nitrogenCombined sources
Metal bindingi300 – 3001ZincCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseSAAS annotationImported

Keywords - Ligandi

Metal-bindingCombined sourcesSAAS annotation, ZincCombined sourcesSAAS annotation

Enzyme and pathway databases

BioCyciBAMB339670:GH48-4693-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Adenosine deaminaseImported (EC:3.5.4.4Imported)
Gene namesi
Ordered Locus Names:Bamb_4621Imported
OrganismiBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))Imported
Taxonomic identifieri339670 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
Proteomesi
  • UP000000662 Componenti: Chromosome 2

Interactioni

Protein-protein interaction databases

STRINGi339670.Bamb_4621.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GXWX-ray1.30A/B2-366[»]
ProteinModelPortaliQ0B6Q2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 349322A_deaminaseInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adenosine and AMP deaminases family.SAAS annotation

Phylogenomic databases

eggNOGiENOG4105EKD. Bacteria.
COG1816. LUCA.
HOGENOMiHOG000218813.
KOiK01488.
OMAiRIAYEFC.
OrthoDBiEOG6BPDDD.

Family and domain databases

InterProiIPR001365. A/AMP_deaminase_dom.
IPR006330. Ado/ade_deaminase.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR01430. aden_deam. 1 hit.

Sequencei

Sequence statusi: Complete.

Q0B6Q2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGTPGNVPA ARTGIEITAA HRAFFHALPK VELHCHLLGA VRHDTFVALA
60 70 80 90 100
QRSGAPIERA EIDAFYARGE KPVGVLHVLR ALDRYLLTRP DDLRRIAYEY
110 120 130 140 150
LEDAAAHNVR HAEFFWNPTG TVRVSGIPYA DAQAAIVTGM RDAARDFGIG
160 170 180 190 200
ARLIPSIDRE QDPDEAVAIV DWMKANRADE VAGIGIDYRE NDRPPELFWK
210 220 230 240 250
AYRDARAAGF RTTAHAGEFG MPWRNVETAV DLLHVDRVDH GYTIVDNPEL
260 270 280 290 300
CARYAERGIV FTVVPTNSYY LRTLPPDQWA ERHPMRKMPG LGLKIHPNTD
310 320 330 340 350
DPTLHKVNPS EAWELMFSHF GFTIADLKQF MLNGIDGAWV DDDTKAAWRA
360
AWAPEFDMLA DTLAAD
Length:366
Mass (Da):41,016
Last modified:October 17, 2006 - v1
Checksum:iE6BFBB1852A5520F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000441 Genomic DNA. Translation: ABI90171.1.
RefSeqiWP_011659583.1. NZ_CP009799.1.

Genome annotation databases

EnsemblBacteriaiABI90171; ABI90171; Bamb_4621.
KEGGibam:Bamb_4621.
PATRICi19025167. VBIBurAmb61564_4839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000441 Genomic DNA. Translation: ABI90171.1.
RefSeqiWP_011659583.1. NZ_CP009799.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GXWX-ray1.30A/B2-366[»]
ProteinModelPortaliQ0B6Q2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi339670.Bamb_4621.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI90171; ABI90171; Bamb_4621.
KEGGibam:Bamb_4621.
PATRICi19025167. VBIBurAmb61564_4839.

Phylogenomic databases

eggNOGiENOG4105EKD. Bacteria.
COG1816. LUCA.
HOGENOMiHOG000218813.
KOiK01488.
OMAiRIAYEFC.
OrthoDBiEOG6BPDDD.

Enzyme and pathway databases

BioCyciBAMB339670:GH48-4693-MONOMER.

Family and domain databases

InterProiIPR001365. A/AMP_deaminase_dom.
IPR006330. Ado/ade_deaminase.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR01430. aden_deam. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.
    , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-244 / AMMDImported.
  2. "Crystal structure of a cog1816 amidohydrolase (target EFI-505188) from Burkhoderia ambifaria, with bound Zn."
    Enzyme Function Initiative (EFI)
    Vetting M.W., Goble A.M., Morisco L.L., Wasserman S.R., Sojitra S., Imker H.J., Raushel F.M., Gerlt J.A., Almo S.C.
    Submitted (SEP-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 2-366 IN COMPLEX WITH ZINC.

Entry informationi

Entry nameiQ0B6Q2_BURCM
AccessioniPrimary (citable) accession number: Q0B6Q2
Entry historyi
Integrated into UniProtKB/TrEMBL: October 17, 2006
Last sequence update: October 17, 2006
Last modified: July 6, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.