ID A0A401JEP9_9PROT Unreviewed; 608 AA.
AC A0A401JEP9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=SFMTTN_1919 {ECO:0000313|EMBL:GBL46107.1};
OS Sulfuriferula multivorans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sulfuricellaceae; Sulfuriferula.
OX NCBI_TaxID=1559896 {ECO:0000313|EMBL:GBL46107.1, ECO:0000313|Proteomes:UP000286806};
RN [1] {ECO:0000313|Proteomes:UP000286806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTN {ECO:0000313|Proteomes:UP000286806};
RA Watanabe T., Kojima H., Fukui M.;
RT "Whole-genome sequencing of sulfur-oxidizing chemolithoautotrophs
RT representing nine proteobacterial species.";
RL Submitted (JUN-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:GBL46107.1}.
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DR EMBL; BGOW01000016; GBL46107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401JEP9; -.
DR Proteomes; UP000286806; 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 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 335..426
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT DOMAIN 470..591
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 608 AA; 66271 MW; 8551B84B32B5E8E5 CRC64;
MQLPIQTYLA DLYQRLFPLQ EGELASYIPE LTRANPDWFG LCIVTMDGFA YTEGDWGQPF
TIQSVSKPFV YALALADRGV DEVMAKVGVE PSGDAFNSIS LDPQTGAPRN PMINAGAIAS
TSLVAGATST QQWQRLQATL SAFAGHELAL DEAVYHSESE TGFRNRAIAW MLRNFGITEG
DPMPSLENYF RQCSLLVDCR DLAYMAATLA NGGIHPLSGQ RCMPAEHVER VLSVMATCGM
YDYAGSWLYE VGMPAKSGVG GGILAVLPGR FGIGVFSPRL DDKGNSVRGI AACKQIAHDF
GLNIFNHTNS PALTVRRIYN AAVSPSHRQT GHHSMAYLRE RADRIKILCL QGELGVDSAE
YVIRQLQHLA PTTDSFILDL HLVANLSNGA ATLLHQARRE LYTAGIAIVL SRIHGRNGIE
ETLSKTTTDA TFGFLCFEGN DLAVQWCENR MLEEFCGEDE IECCYEDSVF FAGIPAPVMA
RLCPLMQTRN FAPGEVILDA GQPSDGQIFF LESGRVNVLA PLAGGGYQFL ATLGPGMNFG
ELVLLGQCTR TAMVHAESET RCRVLAMDDL NTLARELPDL KIAILKNLSL DLADKLKHAT
QMITVLAN
//
