ID A3M037_PICST Unreviewed; 372 AA.
AC A3M037;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 96.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364, ECO:0000256|RuleBase:RU004356};
DE EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937, ECO:0000256|RuleBase:RU004356};
GN Name=GLN1 {ECO:0000313|EMBL:ABN68646.1};
GN ORFNames=PICST_68474 {ECO:0000313|EMBL:ABN68646.1};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN68646.1, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN68646.1, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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:0000256|ARBA:ARBA00000777,
CC ECO:0000256|RuleBase:RU004356};
CC -!- SUBUNIT: Homooctamer. {ECO:0000256|ARBA:ARBA00011823}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC ECO:0000256|RuleBase:RU000384}.
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DR EMBL; CP000502; ABN68646.1; -; Genomic_DNA.
DR RefSeq; XP_001386675.1; XM_001386638.1.
DR AlphaFoldDB; A3M037; -.
DR STRING; 322104.A3M037; -.
DR GeneID; 4840996; -.
DR KEGG; pic:PICST_68474; -.
DR eggNOG; KOG0683; Eukaryota.
DR HOGENOM; CLU_036762_1_1_1; -.
DR InParanoid; A3M037; -.
DR OMA; DRRPNAN; -.
DR OrthoDB; 1115057at2759; -.
DR Proteomes; UP000002258; Chromosome 8.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR008147; Gln_synt_N.
DR InterPro; IPR036651; Gln_synt_N_sf.
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; IPR027302; Gln_synth_N_conserv_site.
DR PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR20852:SF57; GLUTAMINE SYNTHETASE 2 CYTOPLASMIC; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS00180; GLNA_1; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004356};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU004356};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004356};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT DOMAIN 25..104
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 111..372
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT REGION 48..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 41512 MW; 48DDB9D3D97F862F CRC64;
MTTISITEQT AILAKYLELP QNGKVLAEYV WIDSEGNTRS KCRTLAKKPS SVDDLPEWNF
DGSSTGQAPG HDSDVYLRPV AFYPDPFRKG ENIIVLTECW NNDGTPNKFN HRHECAKLMK
AHSDDEVWFG LEQEYTLFDQ FDNVYAWPKG GFPAPQGPYY CGVGTGKVYA RDVIEAHYRA
ALYAGINISG INAEVMPSQW EFQVGPCEGI SMGDELWMAR YLLQRVAEEF GVKISFHPKP
LKGDWNGAGC HTNVSTKSMR VPGGMKDIEV ALSKLAKRHK EHMLLYGADN EQRLTGRHET
ASIDSFSSGV ANRGASIRIP RQVAKEGYGY FEDRRPASNI DPYLVTGIMV ETICGSIPDA
DMSKEFARES SD
//
