ID V8CZR5_9NOCA Unreviewed; 724 AA.
AC V8CZR5;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:ETD32652.1};
GN ORFNames=W823_12280 {ECO:0000313|EMBL:ETD32652.1};
OS Williamsia sp. D3.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Williamsia.
OX NCBI_TaxID=1313067 {ECO:0000313|EMBL:ETD32652.1, ECO:0000313|Proteomes:UP000018666};
RN [1] {ECO:0000313|EMBL:ETD32652.1, ECO:0000313|Proteomes:UP000018666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D3 {ECO:0000313|EMBL:ETD32652.1,
RC ECO:0000313|Proteomes:UP000018666};
RX PubMed=24459282;
RA Guerrero L.D., Makhalanyane T.P., Aislabie J.M., Cowan D.A.;
RT "Draft Genome Sequence of Williamsia sp. Strain D3, Isolated From the
RT Darwin Mountains, Antarctica.";
RL Genome Announc. 2:e01230-13(2014).
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETD32652.1}.
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DR EMBL; AYTE01000018; ETD32652.1; -; Genomic_DNA.
DR RefSeq; WP_023958015.1; NZ_AYTE01000018.1.
DR AlphaFoldDB; V8CZR5; -.
DR PATRIC; fig|1313067.3.peg.2569; -.
DR Proteomes; UP000018666; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.120.1560; -; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR040577; Gln-synt_C.
DR InterPro; IPR008147; Gln_synt_N.
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; IPR022147; GSIII_N.
DR PANTHER; PTHR42974; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR42974:SF1; TYPE-3 GLUTAMINE SYNTHETASE; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF18318; Gln-synt_C-ter; 1.
DR Pfam; PF12437; GSIII_N; 1.
DR SMART; SM01230; Gln-synt_C; 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;
FT DOMAIN 88..181
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 193..620
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 724 AA; 78633 MW; E7923AFF196B0DA9 CRC64;
MSGNNIRLAA ITAVEAYTPP PPSFDTAEAP GDIFGENVFN KSVMLKRLPK NVYKSVMATI
EKGTTLDPAI ADAVASAMKD WALEKGATHY AHVFYPLTGL TAEKHDSFLE PASDGSTLAE
FQGKTLIQGE PDASSFPNGG LRNTFEARGY TGWDVTSPAY VLENPNGNTL CIPTVFVSMT
GEALDHKTPL LRSQQAMGKH AERVLRLFGH SNPGHIVAFC GPEQEYFLVD RHFFLARPDL
INAGRTLFGT KPPKGQEFDD HYFGAIPERV LGFMMDTERE LFKLGIPAKT RHNEVAPGQF
EIAPMFERGN IAADHQQLLM TTFKTVAKKH GMECLFHEKP FEGVNGSGKH VNFSLGNDKF
GSLLVPGDTP HENAQFLVFC AAVIRAVHLH AGLLRVSVAS ATNDHRLGAN EAPPAIVSIF
LGEQLADVFE QIAKGEATSS KGKGTMIIGV DTLPVLPTDP GDRNRTSSFA FTGNRFEFRA
PGSMQTISEP MVVLNTIMAD SLDHCATVLE EAVKEGVQFD TAVQKLLTDI ITEHGAVVFN
GDGYSDTWPI EAESRGLPNL KTTVDALPEL ISAKSIELFS KYGVFNEREM HSRYEIGLEH
YTLTIGVEAK LTLEIGSTLV LPAAVRYQTE LATNVGALKA AGVEADLTLL NALSEPLAAL
TSGLTHLKEA LATHVEGSYE EAVHAKDALL PAMDAVREAA DQIEAQIADD LWPLPTYQEM
LYIL
//
