ID I7L7R4_9CORY Unreviewed; 425 AA.
AC I7L7R4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
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:CCI82792.1};
GN ORFNames=BN46_0034 {ECO:0000313|EMBL:CCI82792.1}, HMPREF9719_00547
GN {ECO:0000313|EMBL:EJZ82559.1};
OS Corynebacterium otitidis ATCC 51513.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=883169 {ECO:0000313|EMBL:CCI82792.1, ECO:0000313|Proteomes:UP000011016};
RN [1] {ECO:0000313|EMBL:CCI82792.1, ECO:0000313|Proteomes:UP000011016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51513 {ECO:0000313|EMBL:CCI82792.1,
RC ECO:0000313|Proteomes:UP000011016};
RX PubMed=23045487; DOI=10.1128/JB.01412-12;
RA Brinkrolf K., Schneider J., Knecht M., Ruckert C., Tauch A.;
RT "Draft Genome Sequence of Turicella otitidis ATCC 51513, Isolated from
RT Middle Ear Fluid from a Child with Otitis Media.";
RL J. Bacteriol. 194:5968-5969(2012).
RN [2] {ECO:0000313|EMBL:EJZ82559.1, ECO:0000313|Proteomes:UP000006078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51513 {ECO:0000313|EMBL:EJZ82559.1,
RC ECO:0000313|Proteomes:UP000006078};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Turicella otitidis ATCC 51513.";
RL Submitted (AUG-2012) 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:CCI82792.1}.
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DR EMBL; CAJZ01000002; CCI82792.1; -; Genomic_DNA.
DR EMBL; AHAE01000030; EJZ82559.1; -; Genomic_DNA.
DR RefSeq; WP_004600437.1; NZ_JH815192.1.
DR AlphaFoldDB; I7L7R4; -.
DR STRING; 29321.AAV33_03050; -.
DR PATRIC; fig|883169.3.peg.517; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_0_0_11; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000006078; Unassembled WGS sequence.
DR Proteomes; UP000011016; 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; 3.30.750.24; STAS domain; 1.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
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 SUPFAM; SSF56601; beta-lactamase/transpeptidase-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:UP000006078}.
FT DOMAIN 319..425
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 404..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 425 AA; 45767 MW; D0478D232B29C2E5 CRC64;
MSTIQSPIPA YLEDLLEQVR DHDAGELADY IPQLKDAEPD RLALALCTVS GRVYSAGDSD
VEFSIQSISK PFVYALALQE LGLEEVRHTV GMEPSGEAFN EMSLEKDTHR PLNPMINVGA
IAVNQLINGP DSSVEDRVER IRSMFSEMAG RELSLDQDLV DAELSGADRN LSLAHMLANY
GKITDEPHDA VLSYIRQCAI EVTVDDLAVM AATLGNGGIQ PVTGKRIFDT AVCRQTMAVM
SAAGMYDQAG RWLAGVGIPA KSGVAGGLIG VLPGQLGIAT FSPRLNDAGN SVRGTALFHK
LSNDMGLHLM NPIAQGTHAV RSIESHGSTT FITLQGTINF AAAERIMHEI QQYGFSGSTI
YVDINRVVAV DPIARRMLAS AMKTMRDEDF NIGLYDPDER LNGLELSDGT EAPVVTSEDI
DEATS
//
