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Database: UniProt
Entry: A0A0C1NAH3_9CYAN
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Original site: A0A0C1NAH3_9CYAN 
ID   A0A0C1NAH3_9CYAN        Unreviewed;       325 AA.
AC   A0A0C1NAH3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
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:KAF3887589.1};
GN   ORFNames=DA73_0214550 {ECO:0000313|EMBL:KIE11707.1}, DA73_0400020420
GN   {ECO:0000313|EMBL:KAF3887589.1};
OS   Tolypothrix bouteillei VB521301.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE11707.1};
RN   [1] {ECO:0000313|EMBL:KIE11707.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VB521301 {ECO:0000313|EMBL:KIE11707.1};
RX   PubMed=25700407;
RA   Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA   Adhikary S.P., Tripathy S.;
RT   "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL   Genome Announc. 3:e00001-15(2015).
RN   [2] {ECO:0000313|EMBL:KAF3887589.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VB521301 {ECO:0000313|EMBL:KAF3887589.1};
RA   Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA   Tripathy S.;
RT   "Improved Assembly of Tolypothrix boutellei genome.";
RL   Submitted (NOV-2019) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:KIE11707.1}.
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DR   EMBL; JHEG04000001; KAF3887589.1; -; Genomic_DNA.
DR   EMBL; JHEG02000043; KIE11707.1; -; Genomic_DNA.
DR   RefSeq; WP_050045628.1; NZ_JHEG04000001.1.
DR   AlphaFoldDB; A0A0C1NAH3; -.
DR   STRING; 1479485.DA73_0214550; -.
DR   OrthoDB; 9788822at2; -.
DR   Proteomes; UP000029738; 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   HAMAP; MF_00313; Glutaminase; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015868; Glutaminase.
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.
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:UP000029738}.
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   325 AA;  36034 MW;  49854E819CB3CD67 CRC64;
     MAKQEELKIT ASSVEPFLSE LHSQYKSLQD GAVANYIPEL SKVNPELFSI CIATVNGEVY
     QVGDYNELFT IQSISKVFVY GLALEDRGRD YLLTKVGVEP TGDAFNAIVL DEVSKRPYNP
     MVNAGAIATT SLIKGTDAIE RLNRMLDMFR RYTGHNVFVD ISVFTSERVT GHRNRAMAHL
     MLNFGTIDQS VDETLDLYFQ QCAVMVNCRD LAVMAATLAN KGINPITREQ SIDSRYIKDI
     LSVMYTCGMY NFAGEWAYKI GIPAKSGISG GIIAVIPNRM GIGVFSPLLD SRGNSIRGVK
     VCEELSQKFG LHLFNCSRQG LQFCE
//
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