ID M4Z9T2_9BRAD Unreviewed; 620 AA.
AC M4Z9T2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=S58_44890 {ECO:0000313|EMBL:BAM90474.1};
OS Bradyrhizobium oligotrophicum S58.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1245469 {ECO:0000313|EMBL:BAM90474.1, ECO:0000313|Proteomes:UP000011841};
RN [1] {ECO:0000313|EMBL:BAM90474.1, ECO:0000313|Proteomes:UP000011841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S58 {ECO:0000313|EMBL:BAM90474.1,
RC ECO:0000313|Proteomes:UP000011841};
RX PubMed=23396330; DOI=10.1128/AEM.00009-13;
RA Okubo T., Fukushima S., Itakura M., Oshima K., Longtonglang A.,
RA Teaumroong N., Mitsui H., Hattori M., Hattori R., Hattori T.,
RA Minamisawa K.;
RT "Genome analysis suggests that the soil oligotrophic bacterium Agromonas
RT oligotrophica (Bradyrhizobium oligotrophicum) is a nitrogen-fixing symbiont
RT of Aeschynomene indica.";
RL Appl. Environ. Microbiol. 79:2542-2551(2013).
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}.
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DR EMBL; AP012603; BAM90474.1; -; Genomic_DNA.
DR RefSeq; WP_015667579.1; NC_020453.1.
DR AlphaFoldDB; M4Z9T2; -.
DR STRING; 1245469.S58_44890; -.
DR KEGG; aol:S58_44890; -.
DR PATRIC; fig|1245469.3.peg.4594; -.
DR eggNOG; COG0659; Bacteria.
DR eggNOG; COG2066; Bacteria.
DR eggNOG; COG2905; Bacteria.
DR HOGENOM; CLU_027932_2_1_5; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000011841; Chromosome.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR015868; Glutaminase.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR NCBIfam; TIGR03814; Gln_ase; 1.
DR PANTHER; PTHR12544; GLUTAMINASE; 1.
DR PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR Pfam; PF01740; STAS; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50801; STAS; 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}.
FT DOMAIN 352..462
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT DOMAIN 487..602
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 620 AA; 67611 MW; 5086F5C599378F40 CRC64;
MTTEQPKPIR HPQHWATAAM PPLQRFLAGC HAEFWPDHDG AVANYIPELG KADPAHFGIS
LATLDGHVYE VGDSRVPFTI QSMSKPFVFA IALDALGSDQ VERVIGVEPS GDPFNSIRLN
AENHPFNPMV NAGAIACSGL VRQARHGDAF ETIRDALGRF AGRRLDVDDA VFTSEAATGD
RNRAIAYLLR TSDVLKEPVD DVLAVYFRQC AVLVTARDCA IMAATLANRG VNPVTGEQVV
TPYAVSRTLA VMTSSGMYDF AGEWIYRVGI PAKSGVGGGI LASLPARLGL GSYSPRLDGH
GNSVRGIKVC EALSAHYGLH MLNRSDDART SIIADYDIGA NPSRRSRRAQ ERDILAAHPD
AVRVLELVGT LSFSNVDYVS RQLAGSARPQ FVIFDLHRVT AMTQAGLRLL AELFRELADF
HVTVVLSGIR RSSAEWQEIT ERTGDLGNVR DFYLLDTAIE WAEDQIVYRY GGAIDFIETT
ELAEQPLLAG LSGDERHELA ALATIKHYQQ GERILAAGEP ANSLFFLRSG VIHVTLPDGI
RLATLTAGQC FGEMALLEPL RSADVVADFS ATAFEITLDD FERFRARHPK AGERIMRNLA
QLLAERLTIA NARLNLLAAD
//
