Skip Header

Contribute Send feedback
Read comments (?) or add your own

B6VKL9 (B6VKL9_PHOAA) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Transforms N(2)-succinylglutamate into succinate and glutamate By similarity. HAMAP-Rule MF_00767 SAAS SAAS016681

Catalytic activity

N-succinyl-L-glutamate + H2O = succinate + L-glutamate. HAMAP-Rule MF_00767 SAAS SAAS016681

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00767 SAAS SAAS016681

Pathway

Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. HAMAP-Rule MF_00767 SAAS SAAS016681

Sequence similarities

Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily. HAMAP-Rule MF_00767

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site2111 By similarity HAMAP-Rule MF_00767
Metal binding511Zinc By similarity HAMAP-Rule MF_00767
Metal binding541Zinc By similarity HAMAP-Rule MF_00767
Metal binding1481Zinc By similarity HAMAP-Rule MF_00767

Sequences

Sequence LengthMass (Da)Tools
B6VKL9 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 3A966092CBC83CFF

FASTA32736,879
        10         20         30         40         50         60 
MDLLTLLLEK KLADHLRFPE TISASWLAEG VLQLIPDKRK NRSLVVSVGI HGNETAPIEI 

        70         80         90        100        110        120 
LIQLLAQLAD GTLTLENNLL IIFGNLPAIR ANRRYLHNDL NRMFGGRYLN FPLGNERSRA 

       130        140        150        160        170        180 
AELENVVSRF FAEPSVSATN IRWHIDLHTA IRASHHEQFA LLPAQGRPFS AEFMQWLSDS 

       190        200        210        220        230        240 
NIEALVYHKE KGGTFSHFLG EKFGTDSCTM EIGKVMPFGK NDLKRFQKVI EALHGLIDHS 

       250        260        270        280        290        300 
QITARTKPEL KHYQVVDSII KSDDSFQLHI PADTMNFTEL PAGFEIASQR DRHWKITSSV 

       310        320 
NFILFPNAEV ANGLRAGLLL ALNKKNN

« Hide

References

« Hide 'large scale' references
[1]"Rapid virulence annotation (RVA): identification of virulence factors using a bacterial genome library and multiple invertebrate hosts."
Waterfield N.R., Sanchez-Contreras M., Eleftherianos I., Dowling A., Yang G., Wilkinson P., Parkhill J., Thomson N., Reynolds S.E., Bode H.B., Dorus S., Ffrench-Constant R.H.
Proc. Natl. Acad. Sci. U.S.A. 105:15967-15972(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 43949 EMBL CAR66699.1.
[2]Crossman L.C.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC43949 EMBL CAQ83593.1.
[3]Thomson N.R.
Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 43949 EMBL CAR66699.1.
[4]"Comparative genomics of the emerging human pathogen Photorhabdus asymbiotica with the insect pathogen Photorhabdus luminescens."
Wilkinson P., Waterfield N.R., Crossman L., Corton C., Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L., Doggett J., Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Arrowsmith C., Churcher C., Harris D. expand/collapse author list , Thompson N.R., Quail M., Parkhill J., Ffrench-Constant R.H.
BMC Genomics 10:302-302(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43949 / 3105-77 and ATCC43949 EMBL CAQ83593.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM162591 Genomic DNA. Translation: CAQ83593.1.
FM211045 Genomic DNA. Translation: CAR66699.1.
RefSeqYP_003040338.1. NC_012962.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING291112.PAU_01501.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ83593; CAQ83593; PAU_01501.
GeneID13861068.
KEGGpay:PAU_01501.
PATRIC20496814. VBIPhoAsy71438_1678.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000280300.
KOK05526.
OMAYLHNDLN.
ProtClustDBPRK05324.

Enzyme and pathway databases

BioCycPASY291112:GJQ0-1564-MONOMER.
UniPathwayUPA00185; UER00283.

Family and domain databases

HAMAPMF_00767. Arg_catab_AstE.
InterProIPR007036. Aste_AspA.
IPR016681. SuccinylGlu_desuccinylase.
[Graphical view]
PfamPF04952. AstE_AspA. 1 hit.
[Graphical view]
TIGRFAMsTIGR03242. arg_catab_astE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB6VKL9_PHOAA
AccessionPrimary (citable) accession number: B6VKL9
Secondary accession number(s): C7BTD3
Entry history
Integrated into UniProtKB/TrEMBL: December 16, 2008
Last sequence update: December 16, 2008
Last modified: May 1, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info