ID A0A1P8UD46_9GAMM Unreviewed; 452 AA.
AC A0A1P8UD46;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:APZ41787.1};
GN ORFNames=BW247_00660 {ECO:0000313|EMBL:APZ41787.1};
OS Acidihalobacter ferrooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Acidihalobacter.
OX NCBI_TaxID=1765967 {ECO:0000313|EMBL:APZ41787.1, ECO:0000313|Proteomes:UP000243807};
RN [1] {ECO:0000313|EMBL:APZ41787.1, ECO:0000313|Proteomes:UP000243807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V8 {ECO:0000313|EMBL:APZ41787.1,
RC ECO:0000313|Proteomes:UP000243807};
RA Khaleque H.N., Ramsay J.P., Murphy R.J.T., Kaksonen A.H., Boxall N.J.,
RA Watkin E.L.J.;
RT "Draft sequence of Acidihalobacter ferrooxidans strain DSM 14175 (strain
RT V8).";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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; CP019434; APZ41787.1; -; Genomic_DNA.
DR RefSeq; WP_076835134.1; NZ_CP019434.1.
DR AlphaFoldDB; A0A1P8UD46; -.
DR STRING; 1765967.BW247_00660; -.
DR OrthoDB; 9789509at2; -.
DR Proteomes; UP000243807; 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 PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF3; GLN-SYNT_C DOMAIN-CONTAINING PROTEIN; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000243807}.
FT DOMAIN 21..110
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 117..452
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 452 AA; 50937 MW; 8718D7DF4EAC16E6 CRC64;
MSINSDEINY INDWFKEHRI TEVECLVPDM TGNARGKIIP ADKFCKEQGM RLPEMLFIQT
VTGDWPDDES MVDPREIDMV LHPDSRTLRK VPWAADPTAQ IIHDCYLRDG APVDIAPRSV
LRGVLDEYAR RGWRPVVAPE LEFYLVQRNT DPDYPLEPPI GRSGRPERAR QSYGIDAVNE
FDPLFEDIYD YCEAQQLDID TLIHESGAAQ MEINFLHGDA MELADQVFLF KRTVREAAMR
HNMYATFMAK PFEDEPGSAM HIHQSIVDTG TGENLFANAD GGLSELFLHY IGGLQAYLPA
TMSLFAPNVN SYRRIAGGES APINADWGTD NRTVGLRVPF ASAPGRRVEN RVVGADANPY
LALAATLACG LLGIIEDIDP RPEQRGSAYD QPFGLPRSLE DALQNLEQAP AELHDLLGRR
FVRAYAAIKR KEYETFFRVI SSWEREFLLL AV
//