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Database: UniProt
Entry: A0A177YFQ0_9NOCA
LinkDB: A0A177YFQ0_9NOCA
Original site: A0A177YFQ0_9NOCA 
ID   A0A177YFQ0_9NOCA        Unreviewed;       608 AA.
AC   A0A177YFQ0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=A3K89_02950 {ECO:0000313|EMBL:OAK54366.1};
OS   Rhodococcus kyotonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=398843 {ECO:0000313|EMBL:OAK54366.1, ECO:0000313|Proteomes:UP000077519};
RN   [1] {ECO:0000313|EMBL:OAK54366.1, ECO:0000313|Proteomes:UP000077519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KB10 {ECO:0000313|EMBL:OAK54366.1,
RC   ECO:0000313|Proteomes:UP000077519};
RA   Jeong H., Hong C.E., Jo S.H., Park J.M.;
RT   "Genome sequence of Rhodococcus kyotonensis KB10.";
RL   Submitted (MAR-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}.
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:OAK54366.1}.
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DR   EMBL; LVHI01000012; OAK54366.1; -; Genomic_DNA.
DR   RefSeq; WP_068424443.1; NZ_LVHI01000012.1.
DR   AlphaFoldDB; A0A177YFQ0; -.
DR   Proteomes; UP000077519; 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; IPR018488; cNMP-bd_CS.
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; 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; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 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:UP000077519}.
FT   DOMAIN          469..571
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;  65041 MW;  B79463B9C08FDCE6 CRC64;
     MTTVVDDILH RIHEACRDEI SGAVADYIPE LAAVSPDGFG IALATSDGYV YEIGDTRAPF
     TIQSISKPFT YGLALADNGE DAVAAKIDIE PSGEPFNEIS LDPVTERPRN PMINAGAITS
     ASLIHGRTAE QRFERIRKAY SRYAGRELTF NDAVYRSEAR TGHRNRAIGY MLRSFDIIAG
     DPDEAVDLYF RQCSIDVTAA DLAMMAATMA NNGVNPRTGE RALSPVLVER VLSVMTTCGM
     YDGAGDWVAK VGLPAKSGVG GGVLAVLPGQ MGIAVYSPRL DGHGNSVRGV AACRQLSRTL
     ELHFLHVPRA AASAVRGRYT VAEAPSRKRR SDIEQDALAK FGHRARVYEL HGDLLFSGAE
     TAVREIGTLD EDLDALVLDV RGVDDVSDIA RSMFDDLRTQ LAAKRCHAAF VDPRGVLGHA
     SSSIDPKDPG GRVFGDIGSG IGWAEELVLD RYCVGPRQPV RISAVEHPVL AGLTEEQYAR
     VEAVTDTRHY AAGDVIVRAG DPAAGLFLVL VGEVSSTYDT PDGFHQRIST LSPGMSFGEM
     PLLANTPFLL NFRADTDLTV AVVTVADFHA LTVDAPATKL AVLGNLAAGA YAQMNIAIKS
     LGQFGVGR
//
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