ID D1PR77_9FIRM Unreviewed; 696 AA.
AC D1PR77;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN Name=glnA {ECO:0000313|EMBL:EFB74779.1};
GN ORFNames=SUBVAR_06905 {ECO:0000313|EMBL:EFB74779.1};
OS Subdoligranulum variabile DSM 15176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Subdoligranulum.
OX NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB74779.1, ECO:0000313|Proteomes:UP000003438};
RN [1] {ECO:0000313|EMBL:EFB74779.1, ECO:0000313|Proteomes:UP000003438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB74779.1,
RC ECO:0000313|Proteomes:UP000003438};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2009) 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:EFB74779.1}.
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DR EMBL; ACBY02000056; EFB74779.1; -; Genomic_DNA.
DR RefSeq; WP_007048255.1; NZ_GG704770.1.
DR AlphaFoldDB; D1PR77; -.
DR STRING; 411471.SUBVAR_06905; -.
DR GeneID; 78307283; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_9; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000003438; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
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 Ligase {ECO:0000313|EMBL:EFB74779.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003438}.
FT DOMAIN 63..152
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 157..585
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 696 AA; 77043 MW; 77710ADBBCCD5C64 CRC64;
MAATVMELYG SKVFNEHEMR ERLPSSTYKS LKATIEKGQP LDLEVANVVA SVMKRWAIEQ
GATHYTHWFQ PLTGITSEKH DGFVSPQPDG TAIMEFSGKE LIKGEPDASS FPSGGLRATA
EARGYTAWDP TSYAFVKDDV LCIPTAFCSY TGEALDKKTP LLRSMQAISD QACKVLHLFG
KDVPRVATTV GPEQEYFLIR KEDYEKRLDI VLTGRTLFGS APSKGQELEE HYFGTIRPIV
SDFMKELDEE LWKLGIPAKT KHNEVAPAQH ELAPIYDTTN VAIDHNLLTM EMMKKIALKH
GLVCLQHEKP FEGVNGSGKH NNWSISTADE NLLDPGDTPM ENLQFMVFLS AVVKAVDEYA
DLLRTSVATP GNDHRLGANE APPAIISIFV GEELEAVIDA VCTDSPYAGP VKMKMDLGVD
VLPKFSKDTT DRNRTSPFAF TGNKFEFRMP GSAENLSDAN TILNTAVAKE LKEFTEETSG
AADFECAAAA WVKKTLNDHR RVIFNGNGYS EAWEAEAERR GLPNRKCTPD AMIALKDPKN
IALMEEFGVL TKTEMLSRYE VEMEHYSKII NIEARTMLKI ANKQLIPAAT SYMGEVANTA
AAKAAAVEGI STKAETKVLQ ALSHYTDEMS DAADELKEVT DKVCALEDES AKAHAFHDEV
LPAMARLRAA ADVAEELVDE EYWPLPCYSR MLFYTE
//