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Glutamine synthetase (GS) (EC 6.3.1.2) (Glutamate--ammonia ligase) (Glutamine synthetase I alpha) (GSI alpha)

 GLN1A_BACSU             Reviewed;         444 AA.
P12425;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 146.
RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:2906311};
Short=GS {ECO:0000303|PubMed:2906311};
EC=6.3.1.2 {ECO:0000269|PubMed:12139611, ECO:0000269|PubMed:24158439};
AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
AltName: Full=Glutamine synthetase I alpha {ECO:0000305};
Short=GSI alpha {ECO:0000305};
Name=glnA {ECO:0000303|PubMed:2906311}; OrderedLocusNames=BSU17460;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2906311; DOI=10.1016/0378-1119(88)90042-X;
Strauch M.A., Aronson A.I., Brown S.W., Schreier H.J.,
Sonenshein A.L.;
"Sequence of the Bacillus subtilis glutamine synthetase gene region.";
Gene 71:257-265(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
STRAIN=ATCC 6633 / PCI 219 / NRS 231;
PubMed=2565853; DOI=10.1016/0378-1097(89)90151-1;
Nakano Y., Tanaka E., Kato C., Kimura K., Horikoshi K.;
"The complete nucleotide sequence of the glutamine synthetase gene
(glnA) of Bacillus subtilis.";
FEMS Microbiol. Lett. 48:81-86(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Borchert S., Klein C., Piksa B., Hammelmann M., Entian K.-D.;
"Sequencing of a 26 kb region of the Bacillus subtilis genome
downstream of spoVJ.";
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[5]
ENZYME REGULATION.
PubMed=4149044;
Deuel T.F., Prusiner S.;
"Regulation of glutamine synthetase from Bacillus subtilis by divalent
cations, feedback inhibitors, and L-glutamine.";
J. Biol. Chem. 249:257-264(1974).
[6]
INDUCTION.
PubMed=2573733; DOI=10.1016/0022-2836(89)90290-8;
Schreier H.J., Brown S.W., Hirschi K.D., Nomellini J.F.,
Sonenshein A.L.;
"Regulation of Bacillus subtilis glutamine synthetase gene expression
by the product of the glnR gene.";
J. Mol. Biol. 210:51-63(1989).
[7]
MUTAGENESIS OF VAL-190, AND ENZYME REGULATION.
PubMed=8093698; DOI=10.1128/jb.175.3.892-897.1993;
Schreier H.J., Rostkowski C.A., Kellner E.M.;
"Altered regulation of the glnRA operon in a Bacillus subtilis mutant
that produces methionine sulfoximine-tolerant glutamine synthetase.";
J. Bacteriol. 175:892-897(1993).
[8]
DISRUPTION PHENOTYPE, AND INDUCTION.
STRAIN=168;
PubMed=8799114; DOI=10.1073/pnas.93.17.8841;
Wray L.V. Jr., Ferson A.E., Rohrer K., Fisher S.H.;
"TnrA, a transcription factor required for global nitrogen regulation
in Bacillus subtilis.";
Proc. Natl. Acad. Sci. U.S.A. 93:8841-8845(1996).
[9]
FUNCTION, INTERACTION WITH TNRA, AND SUBUNIT.
PubMed=11719184; DOI=10.1016/S0092-8674(01)00572-4;
Wray L.V. Jr., Zalieckas J.M., Fisher S.H.;
"Bacillus subtilis glutamine synthetase controls gene expression
through a protein-protein interaction with transcription factor
TnrA.";
Cell 107:427-435(2001).
[10]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF GLY-59; VAL-190; GLY-302; PRO-306 AND GLU-424.
PubMed=12139611; DOI=10.1046/j.1365-2958.2002.03054.x;
Fisher S.H., Brandenburg J.L., Wray L.V. Jr.;
"Mutations in Bacillus subtilis glutamine synthetase that block its
interaction with transcription factor TnrA.";
Mol. Microbiol. 45:627-635(2002).
[11]
SUBCELLULAR LOCATION.
PubMed=17001076; DOI=10.1074/jbc.M607582200;
Heinrich A., Woyda K., Brauburger K., Meiss G., Detsch C., Stuelke J.,
Forchhammer K.;
"Interaction of the membrane-bound GlnK-AmtB complex with the master
regulator of nitrogen metabolism TnrA in Bacillus subtilis.";
J. Biol. Chem. 281:34909-34917(2006).
[12]
X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 2-444 IN COMPLEX WITH
SUBSTRATE ANALOG AND 2 MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-62 AND GLU-304,
ENZYME REGULATION, COFACTOR, AND SUBUNIT.
PubMed=24158439; DOI=10.1074/jbc.M113.519496;
Murray D.S., Chinnam N., Tonthat N.K., Whitfill T., Wray L.V. Jr.,
Fisher S.H., Schumacher M.A.;
"Structures of the Bacillus subtilis glutamine synthetase dodecamer
reveal large intersubunit catalytic conformational changes linked to a
unique feedback inhibition mechanism.";
J. Biol. Chem. 288:35801-35811(2013).
[13]
X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOG AND 2 MAGNESIUM IONS, FUNCTION, INTERACTION WITH TNRA,
MUTAGENESIS OF GLU-424, COFACTOR, AND SUBUNIT.
PubMed=25691471; DOI=10.1101/gad.254714.114;
Schumacher M.A., Chinnam N.B., Cuthbert B., Tonthat N.K., Whitfill T.;
"Structures of regulatory machinery reveal novel molecular mechanisms
controlling B. subtilis nitrogen homeostasis.";
Genes Dev. 29:451-464(2015).
-!- FUNCTION: Glutamine synthetase (GS) is an unusual multitasking
protein that functions as an enzyme, a transcription coregulator,
and a chaperone in ammonium assimilation and in the regulation of
genes involved in nitrogen metabolism (PubMed:25691471). It
catalyzes the ATP-dependent biosynthesis of glutamine from
glutamate and ammonia (PubMed:24158439). Feedback-inhibited GlnA
interacts with and regulates the activity of the transcriptional
regulator TnrA (PubMed:11719184, PubMed:12139611). During nitrogen
limitation, TnrA is in its DNA-binding active state and turns on
the transcription of genes required for nitrogen assimilation
(PubMed:11719184, PubMed:12139611, PubMed:25691471). Under
conditions of nitrogen excess, feedback-inhibited GlnA forms a
stable complex with TnrA, which inhibits its DNA-binding activity
(PubMed:11719184, PubMed:12139611, PubMed:25691471). In contrast,
feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-
binding activity of GlnR, which represses the transcription of
nitrogen assimilation genes (PubMed:25691471).
{ECO:0000269|PubMed:11719184, ECO:0000269|PubMed:12139611,
ECO:0000269|PubMed:24158439, ECO:0000269|PubMed:25691471}.
-!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
L-glutamine. {ECO:0000269|PubMed:12139611,
ECO:0000269|PubMed:24158439}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:24158439,
ECO:0000269|PubMed:25691471};
Note=Binds 2 Mg(2+) ions per subunit.
{ECO:0000269|PubMed:24158439, ECO:0000269|PubMed:25691471};
-!- ENZYME REGULATION: Completely inhibited by glutamine and partially
inhibited by glycine, alanine and AMP (PubMed:4149044,
PubMed:24158439). Also inhibited by L-methionine-SR-sulphoximine
(Met-Sox) (PubMed:8093698, PubMed:24158439).
{ECO:0000269|PubMed:24158439, ECO:0000269|PubMed:4149044,
ECO:0000269|PubMed:8093698}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.18 mM for ammonium {ECO:0000269|PubMed:24158439};
KM=0.83 mM for hydroxylamine {ECO:0000269|PubMed:24158439};
KM=2.3 mM for ATP {ECO:0000269|PubMed:12139611};
KM=2.4 mM for ATP {ECO:0000269|PubMed:24158439};
KM=12 mM for glutamine {ECO:0000269|PubMed:12139611};
KM=24 mM for glutamate {ECO:0000269|PubMed:12139611};
KM=27 mM for glutamate {ECO:0000269|PubMed:24158439};
Vmax=3.7 umol/min/mg enzyme {ECO:0000269|PubMed:24158439};
-!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
hexagons. In its feedback-inhibited form, interacts with TnrA in
order to block its DNA-binding activity. This inhibitory effect is
the highest when both glutamine and AMP are present.
{ECO:0000269|PubMed:11719184, ECO:0000269|PubMed:24158439,
ECO:0000269|PubMed:25691471}.
-!- INTERACTION:
P37582:glnR; NbExp=3; IntAct=EBI-6402863, EBI-6402856;
Q45666:tnrA; NbExp=8; IntAct=EBI-6402863, EBI-8507041;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17001076}.
-!- INDUCTION: Repressed by GlnR under conditions of nitrogen excess
(PubMed:2573733). Repressed by TnrA under conditions of nitrogen
limitation. {ECO:0000269|PubMed:2573733,
ECO:0000269|PubMed:8799114}.
-!- DISRUPTION PHENOTYPE: In cells lacking this gene, expression of
glnR, tnrA, nasB, nrgAB, gabP and ure genes is derepressed.
{ECO:0000269|PubMed:8799114}.
-!- SIMILARITY: Belongs to the glutamine synthetase family.
{ECO:0000305}.
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EMBL; M22811; AAA83376.1; -; Genomic_DNA.
EMBL; D00854; BAA00730.1; -; Genomic_DNA.
EMBL; U66480; AAB41080.1; -; Genomic_DNA.
EMBL; AL009126; CAB13630.1; -; Genomic_DNA.
PIR; JT0392; AJBSQS.
RefSeq; NP_389628.1; NC_000964.3.
RefSeq; WP_003231737.1; NZ_JNCM01000035.1.
PDB; 2FWX; Model; -; A/B/C/D=1-444.
PDB; 4LNF; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L=2-444.
PDB; 4LNI; X-ray; 2.58 A; A/B/C/D/E/F/G/H/I/J/K/L=2-444.
PDB; 4LNK; X-ray; 2.87 A; A/B/C/D/E/F=2-444.
PDB; 4LNN; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L=2-444.
PDB; 4LNO; X-ray; 2.90 A; A/B/C/D/E/F=2-444.
PDB; 4S0R; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-444.
PDBsum; 2FWX; -.
PDBsum; 4LNF; -.
PDBsum; 4LNI; -.
PDBsum; 4LNK; -.
PDBsum; 4LNN; -.
PDBsum; 4LNO; -.
PDBsum; 4S0R; -.
ProteinModelPortal; P12425; -.
SMR; P12425; -.
DIP; DIP-29670N; -.
IntAct; P12425; 4.
MINT; MINT-224371; -.
STRING; 224308.Bsubs1_010100009606; -.
PaxDb; P12425; -.
PRIDE; P12425; -.
EnsemblBacteria; CAB13630; CAB13630; BSU17460.
GeneID; 940020; -.
KEGG; bsu:BSU17460; -.
PATRIC; fig|224308.179.peg.1894; -.
eggNOG; ENOG4105C5F; Bacteria.
eggNOG; COG0174; LUCA.
HOGENOM; HOG000005156; -.
InParanoid; P12425; -.
KO; K01915; -.
OMA; IEAAWNT; -.
PhylomeDB; P12425; -.
BioCyc; BSUB:BSU17460-MONOMER; -.
BRENDA; 6.3.1.2; 658.
SABIO-RK; P12425; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
GO; GO:0070406; F:glutamine binding; IDA:CAFA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008134; F:transcription factor binding; IPI:CAFA.
GO; GO:0043562; P:cellular response to nitrogen levels; IDA:CAFA.
GO; GO:0006542; P:glutamine biosynthetic process; IMP:CACAO.
GO; GO:1904797; P:negative regulation of core promoter binding; IDA:CAFA.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:CAFA.
GO; GO:0090295; P:nitrogen catabolite repression of transcription; IDA:CAFA.
GO; GO:0009399; P:nitrogen fixation; IEA:InterPro.
Gene3D; 3.10.20.70; -; 1.
Gene3D; 3.30.590.10; -; 1.
InterPro; IPR008147; Gln_synt_b-grasp.
InterPro; IPR036651; Gln_synt_N.
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
InterPro; IPR008146; Gln_synth_cat_dom.
InterPro; IPR027303; Gln_synth_gly_rich_site.
InterPro; IPR004809; Gln_synth_I.
InterPro; IPR001637; Gln_synth_I_adenylation_site.
InterPro; IPR027302; Gln_synth_N_conserv_site.
Pfam; PF00120; Gln-synt_C; 1.
Pfam; PF03951; Gln-synt_N; 1.
SMART; SM01230; Gln-synt_C; 1.
SUPFAM; SSF54368; SSF54368; 1.
SUPFAM; SSF55931; SSF55931; 1.
TIGRFAMs; TIGR00653; GlnA; 1.
PROSITE; PS00180; GLNA_1; 1.
PROSITE; PS00182; GLNA_ADENYLATION; 1.
PROSITE; PS00181; GLNA_ATP; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Ligase; Magnesium; Metal-binding;
Nucleotide-binding; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2565853}.
CHAIN 2 444 Glutamine synthetase.
/FTId=PRO_0000153233.
REGION 240 241 L-glutamate binding.
{ECO:0000250|UniProtKB:P9WN39}.
METAL 132 132 Magnesium 1. {ECO:0000244|PDB:4LNF,
ECO:0000244|PDB:4LNI,
ECO:0000244|PDB:4LNK,
ECO:0000244|PDB:4LNN,
ECO:0000244|PDB:4S0R,
ECO:0000269|PubMed:24158439,
ECO:0000269|PubMed:25691471}.
METAL 134 134 Magnesium 2. {ECO:0000244|PDB:4LNF,
ECO:0000244|PDB:4LNI,
ECO:0000244|PDB:4LNK,
ECO:0000244|PDB:4S0R,
ECO:0000269|PubMed:24158439,
ECO:0000269|PubMed:25691471}.
METAL 189 189 Magnesium 2. {ECO:0000244|PDB:4LNF,
ECO:0000244|PDB:4LNI,
ECO:0000244|PDB:4LNK,
ECO:0000244|PDB:4S0R,
ECO:0000269|PubMed:24158439,
ECO:0000269|PubMed:25691471}.
METAL 196 196 Magnesium 2. {ECO:0000244|PDB:4LNF,
ECO:0000244|PDB:4LNI,
ECO:0000244|PDB:4LNK,
ECO:0000244|PDB:4S0R,
ECO:0000269|PubMed:24158439,
ECO:0000269|PubMed:25691471}.
METAL 245 245 Magnesium 1; via pros nitrogen.
{ECO:0000244|PDB:4LNF,
ECO:0000244|PDB:4LNK,
ECO:0000244|PDB:4S0R,
ECO:0000269|PubMed:24158439,
ECO:0000269|PubMed:25691471}.
METAL 333 333 Magnesium 1. {ECO:0000244|PDB:4LNF,
ECO:0000244|PDB:4LNI,
ECO:0000244|PDB:4LNK,
ECO:0000244|PDB:4LNN,
ECO:0000244|PDB:4S0R,
ECO:0000269|PubMed:24158439,
ECO:0000269|PubMed:25691471}.
BINDING 184 184 ATP. {ECO:0000250|UniProtKB:P9WN39}.
BINDING 241 241 L-glutamate; via carbonyl oxygen.
{ECO:0000244|PDB:4LNF,
ECO:0000244|PDB:4LNK,
ECO:0000244|PDB:4LNN,
ECO:0000244|PDB:4S0R,
ECO:0000269|PubMed:24158439,
ECO:0000269|PubMed:25691471}.
BINDING 249 249 ATP. {ECO:0000250|UniProtKB:P77961}.
BINDING 298 298 L-glutamate.
{ECO:0000250|UniProtKB:P0A1P6}.
BINDING 304 304 L-glutamate.
{ECO:0000250|UniProtKB:P0A1P6}.
BINDING 316 316 ATP. {ECO:0000250|UniProtKB:P9WN39}.
BINDING 316 316 L-glutamate.
{ECO:0000250|UniProtKB:P9WN39}.
BINDING 321 321 ATP. {ECO:0000250|UniProtKB:P9WN39}.
BINDING 335 335 L-glutamate.
{ECO:0000250|UniProtKB:P0A1P6}.
SITE 62 62 Important for inhibition by glutamine.
{ECO:0000269|PubMed:24158439}.
VARIANT 10 10 E -> V (in strain: PCI 219).
VARIANT 43 43 G -> E (in strain: PCI 219).
VARIANT 253 253 N -> D (in strain: PCI 219).
VARIANT 259 259 F -> Y (in strain: PCI 219).
MUTAGEN 59 59 G->R: Unable to form stable complex with
TnrA. In the presence of glutamine, this
mutant derepresses amtB-lacZ fusion and
glnRA-lacZ fusion.
{ECO:0000269|PubMed:12139611}.
MUTAGEN 62 62 R->A: Highly resistant to inhibition by
glutamine and AMP. Regulation by TnrA and
GlnR is abolished. Only small differences
(less than 2-fold) in its steady-state
kinetic constants compared with the wild-
type. Similar sensitivity to Met-Sox that
compared to the wild-ytpe.
{ECO:0000269|PubMed:24158439}.
MUTAGEN 190 190 V->A: Unable to form stable complex with
TnrA. In the presence of glutamine, this
mutant partially relieves expression of
the glnRA-lacZ fusion, but has no effect
on the TnrA-dependent regulation of amtB-
lacZ fusion. Resistant to inhibition by
MetSox. {ECO:0000269|PubMed:12139611,
ECO:0000269|PubMed:8093698}.
MUTAGEN 302 302 G->E: Unable to form stable complex with
TnrA. In the presence of glutamine, amtB-
lacZ fusion is only 4-fold regulated by
TnrA, whereas glnRA-lacZ fusion is
derepressed. This mutant retains
enzymatic specific activity with a 2-fold
decrease of the affinity for glutamate
and glutamine compared to the wild-type.
Slightly less sensitive to inhibition by
glutamine. {ECO:0000269|PubMed:12139611}.
MUTAGEN 304 304 E->A: Highly resistant to Met-Sox
inhibition. 8- and 2-fold increase of the
affinity for glutamate and ATP,
respectively. Strong decrease of the
affinity for ammonium.
{ECO:0000269|PubMed:24158439}.
MUTAGEN 306 306 P->H: Unable to form stable complex with
TnrA. In the presence of glutamine, this
mutant completely derepresses glnRA-lacZ
fusion, whereas amtB-lacZ fusion
expression is only partially derepresses.
{ECO:0000269|PubMed:12139611}.
MUTAGEN 424 424 E->K: Unable to form stable complex with
TnrA. In the presence of glutamine, this
mutant derepresses amtB-lacZ fusion and
glnRA-lacZ fusion. Although it is
defective in regulation, this mutant
retains enzymatic specific activity and
similar affinity for ATP, glutamate and
glutamine compared to the wild-type.
Slightly less sensitive to inhibition by
glutamine. {ECO:0000269|PubMed:12139611,
ECO:0000269|PubMed:25691471}.
HELIX 6 16 {ECO:0000244|PDB:4LNI}.
STRAND 20 26 {ECO:0000244|PDB:4LNI}.
STRAND 28 30 {ECO:0000244|PDB:4S0R}.
STRAND 32 38 {ECO:0000244|PDB:4LNI}.
HELIX 39 41 {ECO:0000244|PDB:4LNI}.
HELIX 42 46 {ECO:0000244|PDB:4LNI}.
STRAND 51 53 {ECO:0000244|PDB:4LNI}.
HELIX 54 56 {ECO:0000244|PDB:4LNI}.
HELIX 59 61 {ECO:0000244|PDB:4S0R}.
HELIX 63 65 {ECO:0000244|PDB:4LNI}.
STRAND 67 80 {ECO:0000244|PDB:4LNI}.
HELIX 81 83 {ECO:0000244|PDB:4LNI}.
HELIX 84 87 {ECO:0000244|PDB:4LNI}.
STRAND 89 97 {ECO:0000244|PDB:4LNI}.
STRAND 99 103 {ECO:0000244|PDB:4LNK}.
HELIX 108 121 {ECO:0000244|PDB:4LNI}.
STRAND 125 133 {ECO:0000244|PDB:4LNI}.
STRAND 135 140 {ECO:0000244|PDB:4LNI}.
STRAND 142 144 {ECO:0000244|PDB:4LNN}.
STRAND 146 151 {ECO:0000244|PDB:4LNI}.
TURN 160 162 {ECO:0000244|PDB:4LNI}.
STRAND 163 165 {ECO:0000244|PDB:4LNK}.
HELIX 166 178 {ECO:0000244|PDB:4LNI}.
STRAND 183 188 {ECO:0000244|PDB:4LNI}.
STRAND 194 199 {ECO:0000244|PDB:4LNI}.
HELIX 204 224 {ECO:0000244|PDB:4LNI}.
STRAND 227 230 {ECO:0000244|PDB:4LNI}.
STRAND 244 252 {ECO:0000244|PDB:4LNI}.
STRAND 261 263 {ECO:0000244|PDB:4LNK}.
HELIX 264 266 {ECO:0000244|PDB:4LNI}.
HELIX 269 289 {ECO:0000244|PDB:4LNI}.
HELIX 295 298 {ECO:0000244|PDB:4LNI}.
STRAND 311 313 {ECO:0000244|PDB:4LNI}.
STRAND 316 322 {ECO:0000244|PDB:4LNI}.
HELIX 327 329 {ECO:0000244|PDB:4LNI}.
STRAND 332 334 {ECO:0000244|PDB:4LNI}.
HELIX 343 359 {ECO:0000244|PDB:4LNI}.
HELIX 372 374 {ECO:0000244|PDB:4LNI}.
HELIX 377 383 {ECO:0000244|PDB:4LNI}.
HELIX 392 400 {ECO:0000244|PDB:4LNI}.
HELIX 403 409 {ECO:0000244|PDB:4LNI}.
HELIX 411 430 {ECO:0000244|PDB:4LNI}.
HELIX 434 440 {ECO:0000244|PDB:4LNI}.
TURN 441 443 {ECO:0000244|PDB:4LNI}.
SEQUENCE 444 AA; 50278 MW; 83A5657CE1388AB0 CRC64;
MAKYTREDIE KLVKEENVKY IRLQFTDILG TIKNVEIPVS QLGKALDNKV MFDGSSIEGF
VRIEESDMYL YPDLNTFVIF PWTAEKGKVA RFICDIYNPD GTPFEGDPRN NLKRILKEME
DLGFSDFNLG PEPEFFLFKL DEKGEPTLEL NDKGGYFDLA PTDLGENCRR DIVLELEEMG
FEIEASHHEV APGQHEIDFK YAGAVRSCDD IQTFKLVVKT IARKHGLHAT FMPKPLFGVN
GSGMHCNLSL FKNGVNAFFD ENADLQLSET AKHFIAGIVK HATSFTAVTN PTVNSYKRLV
PGYEAPCYVA WSAQNRSPLI RIPASRGIST RVEVRSVDPA ANPYLALSVL LAAGLDGIKN
KLEAPAPIDR NIYVMSKEER MENGIVDLPA TLAEALEEFK SNEVMVKALG EHLFEHFIEA
KEIEWDMFRT QVHPWEREQY MSQY


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