ID A0A0S9CB47_9MICC Unreviewed; 605 AA.
AC A0A0S9CB47;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=ASE96_18480 {ECO:0000313|EMBL:KQN90872.1};
OS Arthrobacter sp. Leaf69.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN90872.1, ECO:0000313|Proteomes:UP000051467};
RN [1] {ECO:0000313|EMBL:KQN90872.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN90872.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN90872.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN90872.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQN90872.1}.
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DR EMBL; LMLR01000004; KQN90872.1; -; Genomic_DNA.
DR RefSeq; WP_056427087.1; NZ_LMLR01000004.1.
DR AlphaFoldDB; A0A0S9CB47; -.
DR STRING; 1736232.ASE96_18480; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000051467; 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 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 347..421
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT DOMAIN 467..569
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 605 AA; 64658 MW; E245282DD04633C3 CRC64;
MESPIYSYLR RVHAEIAQLK DGSPYNTIPA MANVDPNNFG IALATVDGTV YEIGDTREEF
TIQSISKPFT YGLALEDLGS EAVDAKVDVE PSGDSFNEIS LAEGTGRPAN AMINAGALTA
TSLITGSGGQ SGFKRILSTY SAFAGRQLSV SEKVFESELK HGHRNTALAY LLRSFNIIED
DPTPVLEDYF RQCSVLVNCF DLSIMAATLA NGGRNPLSGK QVLGIGPVER VLSVMMTSGM
YDDAGAWISS VGMPGKSGVA GGIIAVLPGQ VGLAVYSPPL DEHGSSVRGL ATAQRLSRDM
ELHFVRAART GRSAILAAYD VTETPSGIRR NDEAADVLRS HGHRARVIEL NGDLLFAGTE
SMVRELSSLE DDVELVVLDL RRTDQVSEVA LRMLEASRDG LAGAGRELVL IEAHGSVSEA
LGKSAQQPVA SFASRNAAVE YCENRLLERY GNRLLLPDHV PVTASPALAP LDEADAAALE
ALMTPKSFDD GDVIRRVGLR FGGVYFITSG KVSSTSPGPS AERVQLNTLS AGMTFGELAL
GSGSRQETTV RAMGPVELMV LSAEAISELE SADPRLAIAL WKALTRDAYT RVEQYLRESA
VRIRE
//
