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Database: UniProt
Entry: D1PR77_9FIRM
LinkDB: D1PR77_9FIRM
Original site: D1PR77_9FIRM 
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
//
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