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Database: UniProt
Entry: A0A0J1FZY0_9FIRM
LinkDB: A0A0J1FZY0_9FIRM
Original site: A0A0J1FZY0_9FIRM 
ID   A0A0J1FZY0_9FIRM        Unreviewed;       713 AA.
AC   A0A0J1FZY0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KLU68568.1};
GN   ORFNames=RHS_5606 {ECO:0000313|EMBL:KLU68568.1};
OS   Robinsoniella sp. RHS.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Robinsoniella.
OX   NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU68568.1, ECO:0000313|Proteomes:UP000036477};
RN   [1] {ECO:0000313|EMBL:KLU68568.1, ECO:0000313|Proteomes:UP000036477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHS {ECO:0000313|EMBL:KLU68568.1};
RX   PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA   Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA   Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA   Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA   Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT   "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL   Cell 159:253-266(2014).
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:KLU68568.1}.
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DR   EMBL; JNGB01000153; KLU68568.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1FZY0; -.
DR   PATRIC; fig|1504536.3.peg.1701; -.
DR   Proteomes; UP000036477; 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:UP000036477}.
FT   DOMAIN          75..169
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          174..605
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   713 AA;  79491 MW;  F0CE6FE0F92FD0D6 CRC64;
     MAMIEKWRNT MSDNINVAEL FGQNVFNDKV MQERLPKKVY KELHKTIDEG KELDPMIAEV
     VAAAMKEWAV EKGATHYTHW FQPLTGFTAE KHDSFITAPN QDGSILMEFS GKELIKGEPD
     ASSFPSGGLR ATFEARGYTA WDCTSPAFVR EDEGGAILCI PTAFCSYTGE ALDQKTPLLR
     SMQAVQTQAL RLIRLFGNTT SKRVTPSVGV EQEYFIVDRK NYLKRKDLIF TGRTLFGAMP
     PKGQELDDHY FGVIRPRIAK FMKEVNVELW KLGVSSKTQH NEVAPAQHEL APIYAQCNVA
     ADHNQIIMET LKHVAEKQGL QCLLHEKPFA GVNGSGKHNN WSLTTDDGIN LLEPGKTPHE
     NIQFLLILTC ILKAVDIHAD LLRESAADVG NDHRLGANEA PPAIISVFLG EQLEDVLTQL
     ISTGTATHSL KGGRLHTGVK TLPDFNKDAT DRNRTSPFAF TGNKFEFRMV GSRDSVAECN
     VVINTIVAEA FAEACEVLEK ADDFDLAVHD LIKEYASEHE KIVFNGNGYS EEWVEEAKRR
     GLPNITSMVE AIPALVTDKA IELFSKFNVF TKPELESRAE IQYEGYSKAI NIEARAMIDI
     ASKHIIPAVL RYIRNLADTV NAVVQAGLEA QVSIVLLKEA TELLAVTKKE LTHLEEVTEI
     AASKPSGQEQ AMYYYQEVDK AMARLRIPVD QLEMIVDKGE WPMPSYGDLL FEV
//
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