GLN1B_PHOLP
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 25-MAY-2022, entry version 57.
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; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC 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:glutamate-ammonia ligase 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