ID   GLN1B_PHOLP             Reviewed;          23 AA.
AC   P20479;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   08-NOV-2023, entry version 59.
DE   RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P77961};
DE            Short=GS {ECO:0000250|UniProtKB:P77961};
DE            EC=6.3.1.2 {ECO:0000250|UniProtKB:P77961};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:P77961};
DE   AltName: Full=Glutamine synthetase I beta {ECO:0000250|UniProtKB:P77961};
DE            Short=GSI beta {ECO:0000250|UniProtKB:P77961};
DE   Flags: Fragment;
OS   Phormidium lapideum.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Phormidium.
OX   NCBI_TaxID=32060;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2907514; DOI=10.1093/oxfordjournals.jbchem.a122583;
RA   Sawa Y., Ochiai H., Yoshida K., Tanizawa K., Tanaka H., Soda K.;
RT   "Glutamine synthetase from a cyanobacterium, Phormidium lapideum:
RT   purification, characterization, and comparison with other cyanobacterial
RT   enzymes.";
RL   J. Biochem. 104:917-923(1988).
CC   -!- FUNCTION: Involved in nitrogen metabolism via ammonium assimilation.
CC       Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate
CC       and ammonia. {ECO:0000250|UniProtKB:P77961}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC         phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC         Evidence={ECO:0000250|UniProtKB:P77961};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P77961};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P77961};
CC   -!- ACTIVITY REGULATION: The activity of this enzyme could be controlled by
CC       adenylation under conditions of abundant glutamine.
CC       {ECO:0000250|UniProtKB:Q3V5W6}.
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC       {ECO:0000250|UniProtKB:P77961}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000250|UniProtKB:P77961}.
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DR   PIR; PX0011; PX0011.
DR   AlphaFoldDB; P20479; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Ligase;
KW   Nucleotide-binding.
FT   CHAIN           1..>23
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153217"
FT   NON_TER         23
SQ   SEQUENCE   23 AA;  2656 MW;  20B69C164D2A5739 CRC64;
     TTPQEVLSRI KDQGIKLIDL KFI
//