ID A0A3N1CTF2_9ACTN Unreviewed; 594 AA.
AC A0A3N1CTF2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=EDD29_2108 {ECO:0000313|EMBL:ROO84581.1};
OS Actinocorallia herbida.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinocorallia.
OX NCBI_TaxID=58109 {ECO:0000313|EMBL:ROO84581.1, ECO:0000313|Proteomes:UP000272400};
RN [1] {ECO:0000313|EMBL:ROO84581.1, ECO:0000313|Proteomes:UP000272400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44254 {ECO:0000313|EMBL:ROO84581.1,
RC ECO:0000313|Proteomes:UP000272400};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-2018) 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: 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:ROO84581.1}.
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DR EMBL; RJKE01000001; ROO84581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1CTF2; -.
DR Proteomes; UP000272400; Unassembled WGS sequence.
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; 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:UP000272400}.
FT DOMAIN 339..421
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT DOMAIN 461..559
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 594 AA; 63199 MW; 535E4053450357CB CRC64;
MNAPFVSPIK ELLDDLHARL TDRRDGEVAT YIPELGKADP EWLGLAVATL DGTLYEAGDT
DVPFTIQSVS KPFVYALALQ DRGLEDVLKC VGVEPTGDAF NAVRLEPVSG RPYNPMVNSG
AIVTSTLVGG ANQEERRGRI LSGLSAFAGR ALEVDGKVLS SESATGDRNR ALAYLMHGAG
VLTCPVEDAL ALYFEQCAAL VTTRDLAVMT ATLAGGGVNP LTGETVVSVE AAANALTVMA
TCGTYDYAGE WLVRAGLPAK SGVSGGLIAA LPSQLGLGAF SPRLDARGNS VRAVAACEEL
STRFGLHLMR PSERSGPVFH RTLRGDTAHS SRVRAHDERS ALARLGGAIR VYVLRGDLAF
GTAEAVVRTI SEDTDSVRWV VLDLKRAGRV APVAVTLLEG LAAKLKERGI TTVIVDTEKR
VAVRSAVIAE TRDEAMELCE DALLAEAGAA RPEVPIAEQD LLRGLDPFMV TALDAYLETR
EYETGERLVQ DVAALCFILS GGLARQVIIG ERAVRETSMG PGTAVGRLAL IDDAGHSHRI
VAEEPTACKV LTTQSLARLE RDSPRLADAL RWSIANAIAE RLRRTDAENH ALIH
//
