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Database: UniProt/SWISS-PROT
Entry: GLSA_RHOP2
LinkDB: GLSA_RHOP2
Original site: GLSA_RHOP2 
ID   GLSA_RHOP2              Reviewed;         311 AA.
AC   Q2J097;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   01-MAY-2013, entry version 46.
DE   RecName: Full=Glutaminase;
DE            EC=3.5.1.2;
GN   Name=glsA; OrderedLocusNames=RPB_1403;
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the glutaminase family.
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DR   EMBL; CP000250; ABD06113.1; -; Genomic_DNA.
DR   RefSeq; YP_485024.1; NC_007778.1.
DR   ProteinModelPortal; Q2J097; -.
DR   STRING; 316058.RPB_1403; -.
DR   EnsemblBacteria; ABD06113; ABD06113; RPB_1403.
DR   GeneID; 3908353; -.
DR   KEGG; rpb:RPB_1403; -.
DR   PATRIC; 23297373; VBIRhoPal125544_1482.
DR   eggNOG; COG2066; -.
DR   HOGENOM; HOG000216890; -.
DR   KO; K01425; -.
DR   OMA; EPSGNPF; -.
DR   ProtClustDB; PRK00971; -.
DR   BioCyc; RPAL316058:GHF1-1463-MONOMER; -.
DR   GO; GO:0004359; F:glutaminase activity; IEA:HAMAP.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.710.10; -; 1.
DR   HAMAP; MF_00313; Glutaminase; 1; -.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015868; Glutaminase.
DR   PANTHER; PTHR12544; PTHR12544; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF56601; PBP_transp_fold; 1.
DR   TIGRFAMs; TIGR03814; Gln_ase; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase.
FT   CHAIN         1    311       Glutaminase.
FT                                /FTId=PRO_1000048349.
FT   BINDING      66     66       Substrate (By similarity).
FT   BINDING     116    116       Substrate (By similarity).
FT   BINDING     162    162       Substrate (By similarity).
FT   BINDING     169    169       Substrate (By similarity).
FT   BINDING     193    193       Substrate (By similarity).
FT   BINDING     245    245       Substrate (By similarity).
FT   BINDING     263    263       Substrate; via amide nitrogen (By
FT                                similarity).
SQ   SEQUENCE   311 AA;  32999 MW;  2D6B9180FB2F5258 CRC64;
     MNPDLLDHTV AEIAAEMAQR PDRGAVASYI PELAGVDPQR FGLVVIDADG HVAAGGDADM
     PFSIQSISKV FTLTLALGLA GDRVWRRVGR EPSGSAFNSI VQLERERGIP RNPFINAGAI
     AVTDLILSGH QPREALGEIL RFMQFLAGDD SIVIDDAVAA SEQRTGFRNA ALANYMKSFG
     VLDNPVEYTL GVYFHHCAIA MSCRQLALAG RFLAHNGRNP STGHNVVSTQ RARRINALML
     TCGHYDGSGE FAYRVGLPGK SGVGGGVLAV APGKASIAVW SPGLDAAGNS HLGRIALEAL
     TRRLGWSIFG V
//
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