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Database: UniProt
Entry: D2Z7N0_9BACT
LinkDB: D2Z7N0_9BACT
Original site: D2Z7N0_9BACT 
ID   D2Z7N0_9BACT            Unreviewed;       305 AA.
AC   D2Z7N0;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
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=Dpep_1451 {ECO:0000313|EMBL:EFC91477.1};
OS   Dethiosulfovibrio peptidovorans DSM 11002.
OC   Bacteria; Synergistota; Synergistia; Synergistales;
OC   Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX   NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC91477.1, ECO:0000313|Proteomes:UP000006427};
RN   [1] {ECO:0000313|EMBL:EFC91477.1, ECO:0000313|Proteomes:UP000006427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC91477.1,
RC   ECO:0000313|Proteomes:UP000006427};
RX   PubMed=21304695;
RA   Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., Nolan M.,
RA   Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Goodwin L., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type
RT   strain (SEBR 4207).";
RL   Stand. Genomic Sci. 3:85-92(2010).
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|ARBA:ARBA00011881,
CC       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:EFC91477.1}.
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DR   EMBL; ABTR02000001; EFC91477.1; -; Genomic_DNA.
DR   RefSeq; WP_005660903.1; NZ_ABTR02000001.1.
DR   AlphaFoldDB; D2Z7N0; -.
DR   STRING; 469381.Dpep_1451; -.
DR   PaxDb; 469381-Dpep_1451; -.
DR   eggNOG; COG2066; Bacteria.
DR   OrthoDB; 9788822at2; -.
DR   Proteomes; UP000006427; 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:SF29; GLUTAMINASE; 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:UP000006427}.
FT   BINDING         61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   305 AA;  32821 MW;  DF843FC407BC1D5F CRC64;
     MKDILEEISR RSRLKATEGT VASYIPELAK ADPEAFGLAV TECDGSQYLS GNWDHPFTLQ
     SISKIVTLAL ALEERGPERV FSSVGSSPTA DPFNSIMRLE MDAPHRPNNP LINSGAIVVV
     SLLPEEGRER KVDAIMDLCR KLMANDSIDI DDRVYRSEKN TSDRNRSLAY FLRSVGSLNG
     DVEDILDVYF RQCSIKTCAK DLSIMGATFA CDGLNPISGK QIISPSTART VRAIMTTCGM
     YDGSGEFAVK VGIPAKSGVG GGILGTVPGR MGIGVVSPPL DEKGNSVAGL AAMKDISEKL
     RCRVL
//
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