GenomeNet

Database: UniProt/TrEMBL
Entry: B6VKL9_PHOAA
LinkDB: B6VKL9_PHOAA
Original site: B6VKL9_PHOAA 
ID   B6VKL9_PHOAA            Unreviewed;       327 AA.
AC   B6VKL9; C7BTD3;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   19-FEB-2014, entry version 41.
DE   RecName: Full=Succinylglutamate desuccinylase;
DE            EC=3.5.1.96;
GN   Name=astE; OrderedLocusNames=PAU_01501; ORFNames=PA-RVA3-3983;
OS   Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 /
OS   3105-77) (Xenorhabdus luminescens (strain 2)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Photorhabdus.
OX   NCBI_TaxID=553480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 43949;
RX   PubMed=18838673; DOI=10.1073/pnas.0711114105;
RA   Waterfield N.R., Sanchez-Contreras M., Eleftherianos I., Dowling A.,
RA   Wilkinson P., Parkhill J., Thomson N., Reynolds S.E., Bode H.B.,
RA   Dorus S., Ffrench-Constant R.H.;
RT   "Rapid virulence annotation (RVA): identification of virulence factors
RT   using a bacterial genome library and multiple invertebrate hosts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15967-15972(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC43949;
RA   Crossman L.C.;
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 43949;
RA   Thomson N.R.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43949 / 3105-77, and ATCC43949;
RX   PubMed=19583835; DOI=10.1186/1471-2164-10-302;
RA   Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
RA   Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
RA   Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
RA   Harris D., Thompson N.R., Quail M., Parkhill J.,
RA   ffrench-Constant R.H.;
RT   "Comparative genomics of the emerging human pathogen Photorhabdus
RT   asymbiotica with the insect pathogen Photorhabdus luminescens.";
RL   BMC Genomics 10:302-302(2009).
CC   -!- FUNCTION: Transforms N(2)-succinylglutamate into succinate and
CC       glutamate (By similarity).
CC   -!- CATALYTIC ACTIVITY: N-succinyl-L-glutamate + H(2)O = succinate +
CC       L-glutamate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 5/5.
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate
CC       desuccinylase subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; FM162591; CAQ83593.1; -; Genomic_DNA.
DR   EMBL; FM211045; CAR66699.1; -; Genomic_DNA.
DR   RefSeq; YP_003040338.1; NC_012962.1.
DR   STRING; 291112.PAU_01501; -.
DR   EnsemblBacteria; CAQ83593; CAQ83593; PAU_01501.
DR   GeneID; 13861068; -.
DR   KEGG; pay:PAU_01501; -.
DR   PATRIC; 20496814; VBIPhoAsy71438_1678.
DR   HOGENOM; HOG000280300; -.
DR   KO; K05526; -.
DR   OMA; YILFPNA; -.
DR   OrthoDB; EOG613070; -.
DR   ProtClustDB; PRK05324; -.
DR   BioCyc; PASY291112:GJQ0-1564-MONOMER; -.
DR   UniPathway; UPA00185; UER00283.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009017; F:succinylglutamate desuccinylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00767; Arg_catab_AstE; 1.
DR   InterPro; IPR007036; Aste_AspA.
DR   InterPro; IPR016681; SuccinylGlu_desuccinylase.
DR   Pfam; PF04952; AstE_AspA; 1.
DR   TIGRFAMs; TIGR03242; arg_catab_astE; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; Complete proteome; Hydrolase; Metal-binding;
KW   Zinc.
FT   ACT_SITE    211    211       By similarity.
FT   METAL        51     51       Zinc (By similarity).
FT   METAL        54     54       Zinc (By similarity).
FT   METAL       148    148       Zinc (By similarity).
SQ   SEQUENCE   327 AA;  36879 MW;  3A966092CBC83CFF CRC64;
     MDLLTLLLEK KLADHLRFPE TISASWLAEG VLQLIPDKRK NRSLVVSVGI HGNETAPIEI
     LIQLLAQLAD GTLTLENNLL IIFGNLPAIR ANRRYLHNDL NRMFGGRYLN FPLGNERSRA
     AELENVVSRF FAEPSVSATN IRWHIDLHTA IRASHHEQFA LLPAQGRPFS AEFMQWLSDS
     NIEALVYHKE KGGTFSHFLG EKFGTDSCTM EIGKVMPFGK NDLKRFQKVI EALHGLIDHS
     QITARTKPEL KHYQVVDSII KSDDSFQLHI PADTMNFTEL PAGFEIASQR DRHWKITSSV
     NFILFPNAEV ANGLRAGLLL ALNKKNN
//
DBGET integrated database retrieval system