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Database: UniProt
Entry: H1CXL2_9FIRM
LinkDB: H1CXL2_9FIRM
Original site: H1CXL2_9FIRM 
ID   H1CXL2_9FIRM            Unreviewed;       631 AA.
AC   H1CXL2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=GS catalytic domain-containing protein {ECO:0000259|PROSITE:PS51987};
GN   ORFNames=HMPREF9453_00100 {ECO:0000313|EMBL:EHO64043.1};
OS   Dialister succinatiphilus YIT 11850.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Dialister.
OX   NCBI_TaxID=742743 {ECO:0000313|EMBL:EHO64043.1, ECO:0000313|Proteomes:UP000003277};
RN   [1] {ECO:0000313|EMBL:EHO64043.1, ECO:0000313|Proteomes:UP000003277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 11850 {ECO:0000313|EMBL:EHO64043.1,
RC   ECO:0000313|Proteomes:UP000003277};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Lui A.,
RA   MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Dialister succinatiphilus YIT 11850.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01331,
CC       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:EHO64043.1}.
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DR   EMBL; ADLT01000001; EHO64043.1; -; Genomic_DNA.
DR   RefSeq; WP_008858606.1; NZ_JH591187.1.
DR   AlphaFoldDB; H1CXL2; -.
DR   STRING; 742743.HMPREF9453_00100; -.
DR   PATRIC; fig|742743.3.peg.103; -.
DR   eggNOG; COG0174; Bacteria.
DR   HOGENOM; CLU_432584_0_0_9; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000003277; Unassembled WGS sequence.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   PANTHER; PTHR43407; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR43407:SF1; LENGSIN; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000003277}.
FT   DOMAIN          150..554
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   631 AA;  70244 MW;  F5E82B70361CE51B CRC64;
     MNKDLLYYIP TGEFGKEGVL SLLKTHPEIR FVSLVGIDLA GNDTDEKVPI ELFLKNYDDF
     FAGTAVQTDG SSVVLMNIAT LNDARVDMVA DPSVNWYIDY NEDNIYENGR PVGTLRIPCF
     LLHNGKFIDS RSILKDSCAF VADKLKGLLA GGKKVKGMED VPFEDIEDIE FTIGTELEFW
     VKTPSEKETI QHLSISQRLQ EQYWQRMRGN VRTAMEEAIE ELDARGMSVE MGHKEVGGIK
     PKVDDAGHTV DVCEQLELDW RFSMNPLQAA DNELEARIII REVFRKYGLD VSFKAKPIIG
     VAGSGEHTHV GICATLKNGK TINLLAPTEM KADFLSTIGY GFIMGILKNY EATNPFVSST
     TDAFNRLKPG FEAPVCIVTS LGHKPEVPSR NRTILIGLVR DIDNPKATRF ELRAPNPFTN
     TYLAASCLFL SALDGITYAV TSGKTPADLL AELSKKPGEK ADYLEEGRAY RCEDNVFEDF
     TQEERDAAFG KPPATVWENV KTMKANPDKV AVIEAGGTLN ATIVDSFVAS IVYRWKNELI
     DRIIPATEAL VKGFKKLSSE DDLDEERWAD ILDKKYELIK DTKAGKSLCT KLKDALEADD
     YDTASDLQIE INKKAEALEK EYGEYALNIV G
//
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