ID A1S4S5_SHEAM Unreviewed; 455 AA.
AC A1S4S5;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=L-glutamine synthetase {ECO:0000313|EMBL:ABL99381.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:ABL99381.1};
GN OrderedLocusNames=Sama_1174 {ECO:0000313|EMBL:ABL99381.1};
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297 {ECO:0000313|EMBL:ABL99381.1, ECO:0000313|Proteomes:UP000009175};
RN [1] {ECO:0000313|EMBL:ABL99381.1, ECO:0000313|Proteomes:UP000009175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) 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:PRU01331, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; CP000507; ABL99381.1; -; Genomic_DNA.
DR RefSeq; WP_011759290.1; NC_008700.1.
DR AlphaFoldDB; A1S4S5; -.
DR STRING; 326297.Sama_1174; -.
DR DNASU; 4603426; -.
DR KEGG; saz:Sama_1174; -.
DR eggNOG; COG0174; Bacteria.
DR HOGENOM; CLU_017290_0_0_6; -.
DR OrthoDB; 9789509at2; -.
DR Proteomes; UP000009175; Chromosome.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
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: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; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:ABL99381.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000009175}.
FT DOMAIN 120..455
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 455 AA; 50500 MW; AE8307C73250B03C CRC64;
MPFANPQEAI DFLDKHPQVQ HVEVFIIDPN GIPRGKLLHR QEVLSMYRHG RPLPSTILGL
TVQGDDVEDT GLVWEVGDAD CLAFPIEGGL LMQPWRAQPT AQVHLTMHPE AGMPAAVADP
RLVLSKVIDS LQADGFYPVM AAELEFFLLD QRFDANGRPQ PAMQSDGHRP HQTQVYGILE
LERLQPFLDD LYHACEVQGI PARTAISEYA PGQVEITLEH RFDALQAMDE AVRYKRLVKG
VAAKHGMQAC FMAKPFGELA GSGMHMHVSL ADADGNNRFA SDNPEGTPEL TQSIAGMMAT
LEDAQLLFCP NANSFRRFQS ASYAPIAKTW GVNNRTVSFR VPGGPAPSRH VEHRICGADA
NPYLAAAAIL AACHHGIRNQ LSPGQAIVGN GYEGKHQTLP TDWLSALTNF ERSEWMKSVL
GEDFHRIYGR IKRAEYQEFM AEVGQQDWHW YLTHA
//
