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Database: UniProt
Entry: A0A171KTT7_9BURK
LinkDB: A0A171KTT7_9BURK
Original site: A0A171KTT7_9BURK 
ID   A0A171KTT7_9BURK        Unreviewed;       319 AA.
AC   A0A171KTT7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Glutaminase {ECO:0000256|ARBA:ARBA00012918, ECO:0000256|HAMAP-Rule:MF_00313};
DE            EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918, ECO:0000256|HAMAP-Rule:MF_00313};
GN   Name=glsA {ECO:0000256|HAMAP-Rule:MF_00313};
GN   ORFNames=AAV32_04120 {ECO:0000313|EMBL:KKO72304.1}, EV679_1781
GN   {ECO:0000313|EMBL:RZS70375.1};
OS   Kerstersia gyiorum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Kerstersia.
OX   NCBI_TaxID=206506 {ECO:0000313|EMBL:KKO72304.1, ECO:0000313|Proteomes:UP000078084};
RN   [1] {ECO:0000313|EMBL:KKO72304.1, ECO:0000313|Proteomes:UP000078084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1 {ECO:0000313|EMBL:KKO72304.1,
RC   ECO:0000313|Proteomes:UP000078084};
RA   Greninger A.L., Kozyreva V., Chaturvedi V.;
RT   "Genome sequence of Kerstersia gyiorum CG1.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RZS70375.1, ECO:0000313|Proteomes:UP000292039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16618 {ECO:0000313|EMBL:RZS70375.1,
RC   ECO:0000313|Proteomes:UP000292039};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001062, ECO:0000256|HAMAP-
CC         Rule:MF_00313};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00313}.
CC   -!- SIMILARITY: Belongs to the glutaminase family.
CC       {ECO:0000256|ARBA:ARBA00011076, ECO:0000256|HAMAP-Rule:MF_00313}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKO72304.1}.
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DR   EMBL; LBNE01000002; KKO72304.1; -; Genomic_DNA.
DR   EMBL; SGWZ01000002; RZS70375.1; -; Genomic_DNA.
DR   RefSeq; WP_068367950.1; NZ_VZPC01000005.1.
DR   AlphaFoldDB; A0A171KTT7; -.
DR   STRING; 206506.AAV32_04120; -.
DR   GeneID; 73001188; -.
DR   PATRIC; fig|206506.3.peg.895; -.
DR   OrthoDB; 9788822at2; -.
DR   Proteomes; UP000078084; Unassembled WGS sequence.
DR   Proteomes; UP000292039; Unassembled WGS sequence.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   HAMAP; MF_00313; Glutaminase; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015868; Glutaminase.
DR   NCBIfam; TIGR03814; Gln_ase; 1.
DR   PANTHER; PTHR12544; GLUTAMINASE; 1.
DR   PANTHER; PTHR12544:SF48; GLUTAMINASE 1; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|HAMAP-Rule:MF_00313};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00313};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078084}.
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   319 AA;  33564 MW;  7BE60E3D9286A529 CRC64;
     MPTPPSIQRA VDDAFQAFGQ LPGGANADYI PFLAQVPDKL SALAVVGIDG SQYCAGDVRY
     RFALESISKV CTLALALEDW GHDTVQEKIG ADATGLPFNS IMALELHAGK PLSPLVNAGA
     IATASLVKAG SVEERWQRIL AIQQQLGSGE IALSAELNES EQSTNAHNRA IAWLLHSAGY
     MYCDPMEACD VYTRQCSTLL DCLELATIGA TLASGGLHPF SGKRVLQAEN TPRILADMTM
     EGLYDSSGDW AYTVGLPGKS GVGGGLLAVV PGVLAIAAFS PPLDEFGNSV RGQKMIAAVA
     DTLGYNIYRS PATALPHSR
//
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