ID A0A1I7MMI8_9MICC Unreviewed; 635 AA.
AC A0A1I7MMI8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN04487966_10662 {ECO:0000313|EMBL:SFV23143.1};
OS Micrococcus terreus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=574650 {ECO:0000313|EMBL:SFV23143.1, ECO:0000313|Proteomes:UP000198881};
RN [1] {ECO:0000313|EMBL:SFV23143.1, ECO:0000313|Proteomes:UP000198881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7054 {ECO:0000313|EMBL:SFV23143.1,
RC ECO:0000313|Proteomes:UP000198881};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FPCG01000006; SFV23143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7MMI8; -.
DR STRING; 574650.SAMN04487966_10662; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000198881; 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; PF00027; cNMP_binding; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-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:UP000198881}.
FT DOMAIN 347..473
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT DOMAIN 498..587
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 114
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 635 AA; 68733 MW; D2A7E1CE59156B08 CRC64;
MEFPVQIYLD RLARDMREVE GGTPYQGIPA TAEMDPALYG VSLTTVDGHS YAAGDSDHLF
SLQSISKALT YGMALDDLGT EDVLAKIDVE PSGDPFNEIS LQSGTGRPDN PMINAGAIAT
TSLIKGRGGR DRMGRILMTF SAAAGRELKV SEQVFRSEDR TGHRNRAMAW LLRSFDIIES
DPEPIVQDYF RQCSVMVTAE DLSMMAATLA NQGVNPASGE RVFTPHTVRW MLSVMSTCGM
YDDAGTWAIE VGLPAKSGVG GGVLVVVPGQ LGIGVFSPPL DEHGTSVRGA QTVRQLADDL
GLHYSDAPPV GRSTIRSDYR LADTPSGVPR TPEATQALET HGQMCRILEL GGDMGFAETE
TLARVVVETD ETDPSTEMVM LDLRKVDDFG RAAVAIFARL IRELLSSGTD VILVDEEDAL
TQRVLERAAS SGEGALPDPL SPEEDRRAAL RDAESTTAEF QLFLTRAQAV EWAEHRILAR
HAPDLLPANA QQPLTSSVMQ MMSPADAEQL SVFLEPRTYK PGQVIRRAGQ PFGGIYFITS
GQVELTGQGS GKRRYRQVFL SPGMTFGEIA LGQAGRQLST VRAVGEVTTQ VLTAQLISAL
EETDPQLAIK LWSALARDAY TMVEQAFRET GARDS
//
