ID GLNA_STRCO Reviewed; 469 AA.
AC P15106;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 01-MAY-2013, entry version 99.
DE RecName: Full=Glutamine synthetase;
DE EC=6.3.1.2;
DE AltName: Full=Glutamate--ammonia ligase;
GN Name=glnA; OrderedLocusNames=SCO2198; ORFNames=SC3H12.06;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Streptomycineae; Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2906310; DOI=10.1016/0378-1119(88)90041-8;
RA Wray L.V. Jr., Fisher S.H.;
RT "Cloning and nucleotide sequence of the Streptomyces coelicolor gene
RT encoding glutamine synthetase.";
RL Gene 71:247-256(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces
RT coelicolor A3(2).";
RL Nature 417:141-147(2002).
CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC L-glutamine.
CC -!- ENZYME REGULATION: The activity of this enzyme is controlled by
CC adenylation under conditions of abundant glutamine. The fully
CC adenylated enzyme complex is inactive (By similarity).
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
CC hexagons.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Regulated in response to the available nitrogen source.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
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DR EMBL; M23172; AAA72717.1; -; Genomic_DNA.
DR EMBL; AL939111; CAB90845.1; -; Genomic_DNA.
DR PIR; JT0389; AJSMQC.
DR RefSeq; NP_626450.1; NC_003888.3.
DR ProteinModelPortal; P15106; -.
DR SMR; P15106; 3-469.
DR STRING; 100226.SCO2198; -.
DR PhosSite; P12011306; -.
DR EnsemblBacteria; CAB90845; CAB90845; CAB90845.
DR GeneID; 1097631; -.
DR KEGG; sco:SCO2198; -.
DR PATRIC; 23734052; VBIStrCoe124346_2235.
DR eggNOG; COG0174; -.
DR HOGENOM; HOG000005157; -.
DR KO; K01915; -.
DR OMA; DPSCNGY; -.
DR ProtClustDB; CLSK635529; -.
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:EC.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:InterPro.
DR Gene3D; 3.10.20.70; -; 1.
DR Gene3D; 3.30.590.10; -; 1.
DR InterPro; IPR008147; Gln_synt_beta.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR027303; Gln_synth_gly_rich_site.
DR InterPro; IPR004809; Gln_synth_I.
DR InterPro; IPR001637; Gln_synth_I_adenylation_site.
DR InterPro; IPR027302; Gln_synth_N_conserv_site.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SUPFAM; SSF54368; Gln_synt_beta; 1.
DR TIGRFAMs; TIGR00653; GlnA; 1.
DR PROSITE; PS00180; GLNA_1; 1.
DR PROSITE; PS00182; GLNA_ADENYLATION; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1 469 Glutamine synthetase.
FT /FTId=PRO_0000153266.
FT MOD_RES 397 397 O-AMP-tyrosine (By similarity).
SQ SEQUENCE 469 AA; 52568 MW; 7C141D49C70FC437 CRC64;
MFQNADDVKK FIADEDVKFV DVRFCDLPGV MQHFTLPATA FDPDAEQAFD GSSIRGFQAI
HESDMSLRPD LSTARVDPFR RDKTLNINFF IHDPITGEQY SRDPRNVAKK AEAYLASTGI
ADTAFFGPEA EFYVFDSVRF ATRENESFYH IDSEAGAWNT GALEDNRGYK VRYKGGYFPV
PPVDHFADLR AEISLELERS GLQVERQHHE VGTAGQAEIN YKFNTLLAAA DDLQLFKYIV
KNVAWKNGKT ATFMPKPIFG DNGSGMHVHQ SLWSGGEPLF YDEQGYAGLS DTARYYIGGI
LKHAPSLLAF TNPTVNSYHR LVPGFEAPVN LVYSQRNRSA AMRIPITGSN PKAKRVEFRA
PDASGNPYLA FSALLLAGLD GIKNKIEPAE PIDKDLYELA PEEHANVAQV PTSLGAVLDR
LEADHEFLLQ GDVFTPDLIE TWIDFKRANE IAPLQLRPHP HEFEMYFDV
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