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Database: UniProt
Entry: A0A143Q841_9NOCA
LinkDB: A0A143Q841_9NOCA
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ID   A0A143Q841_9NOCA        Unreviewed;       608 AA.
AC   A0A143Q841;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   ECO:0000313|EMBL:AMY18921.1};
GN   ORFNames=A3Q40_01531 {ECO:0000313|EMBL:AMY18921.1};
OS   Rhodococcus sp. PBTS 1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY18921.1, ECO:0000313|Proteomes:UP000076180};
RN   [1] {ECO:0000313|EMBL:AMY18921.1, ECO:0000313|Proteomes:UP000076180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY18921.1,
RC   ECO:0000313|Proteomes:UP000076180};
RX   PubMed=27284129;
RA   Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT   "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT   Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|Proteomes:UP000076180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA   Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT   "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT   Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
RL   Submitted (APR-2016) 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|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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00313}.
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DR   EMBL; CP015219; AMY18921.1; -; Genomic_DNA.
DR   RefSeq; WP_068100899.1; NZ_CP015219.1.
DR   AlphaFoldDB; A0A143Q841; -.
DR   STRING; 1653478.A3Q40_01531; -.
DR   KEGG; rhu:A3Q40_01531; -.
DR   PATRIC; fig|1653478.3.peg.1541; -.
DR   Proteomes; UP000076180; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076180}.
FT   DOMAIN          347..446
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
FT   DOMAIN          471..573
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   BINDING         64
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   608 AA;  64802 MW;  089E2E5E7EECDD6A CRC64;
     MTDVVQHILD DVYALCAQDT SGAVADYIPE LASAEPERFG ICLTTADGYV YEVGDTRVPF
     TIQSVSKPFT YALALADRGE EAVAAKIDVE PSGEPFNEIS LDPVTERPRN PMIIAGAITA
     ASLVAGDTPG EQFERIRRSF SRFAGRDLEL DAAVHASEAA TGHRNRAIGH MLRSFGVVES
     DPDAAVDLYF RQCSLTVTGR DIALMAATLA NNGTNPCTGV VAADPVLTER VLSVMTTCGM
     YDGAGDWVNR VGLPAKSGVA GSVMAVLPGQ LGISVFSPRL DGHGNSVRGV LACRELSRRL
     ELHFLHVGRA ARSAVRARYS LVDAPSRRRR TASEQRTLAE RGSRARIFEL HGDLLFSAAE
     SVVRAVTPAA DETPPDAVVL DMRRVDDVSG VARSMLDALA DQLRTAGCAA GLVDPRGTMA
     HTVSTLADRN GSGRVFATLD SALRWAEDVV LDRWCDGPRQ ATEVSLAEHP VLAAATPDHR
     DGIMALTTTV RHAPGTVVAD VGDPALGLAL VLSGRVTVEF VSDDDVVRPV STLSAGMSFG
     EIPLVRRSEF GLRITAVEDT EVAVLAPADF DRLRVEDPAA TADLVITLLD RAYEQVETIV
     GALRQRTT
//
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