ID A0A1P8XDT4_9MYCO Unreviewed; 440 AA.
AC A0A1P8XDT4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Type III glutamate--ammonia ligase {ECO:0000313|EMBL:AQA04474.1};
GN ORFNames=BVC93_20895 {ECO:0000313|EMBL:AQA04474.1};
OS Mycobacterium sp. MS1601.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1936029 {ECO:0000313|EMBL:AQA04474.1, ECO:0000313|Proteomes:UP000188050};
RN [1] {ECO:0000313|EMBL:AQA04474.1, ECO:0000313|Proteomes:UP000188050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS1601 {ECO:0000313|EMBL:AQA04474.1,
RC ECO:0000313|Proteomes:UP000188050};
RX PubMed=26804932; DOI=10.1016/j.jbiotec.2016.01.022;
RA Sayed M., Dishisha T., Sayed W.F., Salem W.M., Temerk H.A., Pyo S.H.;
RT "Selective oxidation of trimethylolpropane to 2,2-bis(hydroxymethyl)butyric
RT acid using growing cells of Corynebacterium sp. ATCC 21245.";
RL J. Biotechnol. 221:62-69(2016).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; CP019420; AQA04474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8XDT4; -.
DR STRING; 1936029.BVC93_20895; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000188050; Chromosome.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
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; IPR017536; Glutamine_synthetase_typeIII.
DR NCBIfam; TIGR03105; gln_synth_III; 1.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF12; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE PUUA; 1.
DR Pfam; PF00120; Gln-synt_C; 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; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:AQA04474.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842}.
FT DOMAIN 14..98
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 104..440
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 440 AA; 47392 MW; D51DCA59094C149E CRC64;
MAAPTDLAQA AKDTNTKFIL ALFVDLRGKP CAKLVPVEAV DMLVEEGVGF AGYAVGAIGQ
EPKDPDLMAM PDAASFTPIP FIKEGLAIVH CDPHVEGKPW PFAPRVILKS MLARAADSDL
KAYVGAEVEY FLLRRDADGN LCTADPGDSA DQPCYDARGV TRMFDHLSGI STAMNTLGWG
NYANDHEDGN GQFEQNFTYS DALTTADRVI TLRYLLTMLA EQRGMIATFM GKPFSDRTGS
GMHLHLSLRG KDDSPVFPDA DDPRGLGLSS LAYNFLGGIL EHSCALQAVV APTVNAFKRT
GAVSTTSGAS WAPRTPTYGG NDRTHYVRIP DDQRIELRGP DGSANPYLAI AAALGAGLDG
IKRNVDPGEP GASTEQRLQP LPLTLLHAVE ALEADDVISG ALDGAGEGVA AYFANLKREE
FFTWHREVTP WEIDRYLQAF
//
