ID M2YG15_9MICC Unreviewed; 721 AA.
AC M2YG15;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=C884_01520 {ECO:0000313|EMBL:EME37469.1};
OS Kocuria palustris PEL.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1236550 {ECO:0000313|EMBL:EME37469.1, ECO:0000313|Proteomes:UP000009877};
RN [1] {ECO:0000313|EMBL:EME37469.1, ECO:0000313|Proteomes:UP000009877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEL {ECO:0000313|EMBL:EME37469.1,
RC ECO:0000313|Proteomes:UP000009877};
RX PubMed=24504000;
RA Sharma G., Khatri I., Subramanian S.;
RT "Draft Genome Sequence of Kocuria palustris PEL.";
RL Genome Announc. 2:e01261-13(2014).
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:EME37469.1}.
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DR EMBL; ANHZ02000003; EME37469.1; -; Genomic_DNA.
DR RefSeq; WP_006213573.1; NZ_ANHZ02000003.1.
DR AlphaFoldDB; M2YG15; -.
DR Proteomes; UP000009877; Unassembled WGS sequence.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
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; 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 SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 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:UP000009877}.
FT DOMAIN 387..463
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 217
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 293
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 721 AA; 78601 MW; 43A1DA0E3469F2EE CRC64;
MTSHDRQQRH ETAQNTDDDQ GTSYQLDENG DPLGWADTQR PSPEWSESEK LFGPSPIEGA
LAAVLDEVRE LTEGEPSSSI PALANADPEK LAVVVATAGG HIYEAGDSRD CFSIQSISKA
FVYGLAIEDR GFGGVDAKID VEPSGESFNR ISLHPETNRP ANAMINAGAI TASWLVDPHR
GTARRERVRQ LFSAFAGREL MMDPDVYSQE HKEGDRNRAL GWMLSSVGII EEDPTQALED
YFAQCSVMVD TRDLAIMGAT LAAGGRNPFT DERVMEPVTV ERVLSVMNSC GMYDDAGEWF
VRVGLPGKSG VGGGIIAVVP GQLAVATFAP PLDQHGNSVR GTAACERISQ AMDLHFARGP
RPSKRTVRSI HSLADARSLT HRDEDSRRAL SELASDVAVI EIQGNLLFPG TEETVRALRQ
SAQTASSVIL DLSDVDQIAG FGRHLIAVTA TELCEAGRDV ALVVGDPWTD DWHDAWDTVW
EDIWRDEPDD DPDGPSNPYT DSLPAISAAR KIRTTTKPEN LTVFATREEA LAHVEDQLIE
QLRRRDDDAT ASDADEMPDL DAESTIEAAR STDLLRDTDD EIAETIWSRA QELRVREGEP
VLDLEPGESA VVLVVEGLVE MIPHGSHEDG SVVRRMRPGT VFRSSGVSDE RLSVQAVAGT
DLVVRVLDAP ALRALEQEEP AAALELWRSM ARAASEDLET ALRANIGWEP GDHWNETPVE
D
//
