ID A0A0Q6FJ90_9ACTN Unreviewed; 725 AA.
AC A0A0Q6FJ90;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:KQT94361.1};
GN ORFNames=ASG49_05630 {ECO:0000313|EMBL:KQT94361.1};
OS Marmoricola sp. Leaf446.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Marmoricola.
OX NCBI_TaxID=1736379 {ECO:0000313|EMBL:KQT94361.1, ECO:0000313|Proteomes:UP000051542};
RN [1] {ECO:0000313|EMBL:KQT94361.1, ECO:0000313|Proteomes:UP000051542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT94361.1,
RC ECO:0000313|Proteomes:UP000051542};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT94361.1, ECO:0000313|Proteomes:UP000051542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT94361.1,
RC ECO:0000313|Proteomes:UP000051542};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQT94361.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMRF01000001; KQT94361.1; -; Genomic_DNA.
DR RefSeq; WP_056538152.1; NZ_LMRF01000001.1.
DR AlphaFoldDB; A0A0Q6FJ90; -.
DR STRING; 1736379.ASG49_05630; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000051542; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000051542}.
FT DOMAIN 88..181
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 197..620
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 725 AA; 78531 MW; D2A45FC7126CEC1E CRC64;
MTANQVRLQA IKGVESTVPP AYSFDPGEEP GQIFGENVFS LNVMQKRLPK GVYKSVVSTI
EKSTPLDPDV ADAVASAMKD WAMEKGATHY AHVFYPLTGL TAEKHDSFLD PVGDGTAFAS
FSGKTLVQGE PDASSFPNGG LRNTFEARGY TGWDVMSPAY VLENPNGNTL CIPTIFISMT
GEALDHKTPV LRSQQAMSAQ AKRVLRLFGH DDPDNVVAYC GPEQEYFLVD SHFFTARPDL
LNAGRTLFGA KPPKGQEFDD HYFGAIPERV LGFMMDTERE LFKLGIPAKT RHNEVAPGQF
EVAPMFERAN EASDHQQLLM TTFKSVARKH GMECLFHEKP FDGVNGSGKH VNFSLGNAEL
GSLLVPGDNP HDNAQFLVFC AAVVRAVHQY GGLLRSSVAS AGNDHRLGAN EAPPAIISIF
LGDQLADVFD QIAKGGATHS KEKGTLTIGV DTLPNLSKDP GDRNRTSPFA FTGNRFEFRA
PGSNQTVAGP MVVLNTIMAE ALDHAATYLE DAVAAGTDFN EAVQSLLTEI VTEHGKVIFN
GNGYSDEWPV EAEQRGLKNL RTTVDALPEL ITPEALALFA KYDVFNDREM HSRYEIGLEQ
YVLSISVEAN LTLEMGTTIV LPAAVRYQTE LATNVSALKA AGVDADLADL EAVSVPLAAL
RAGLKELAAA VAHEHPEDAM EAATYCRDTV IPAMAAVREA ADTLEGVVAD DLWSLPTYQE
MLYLL
//
