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Database: UniProt
Entry: F0H1B7_9FIRM
LinkDB: F0H1B7_9FIRM
Original site: F0H1B7_9FIRM 
ID   F0H1B7_9FIRM            Unreviewed;       687 AA.
AC   F0H1B7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Glutamate--ammonia ligase, catalytic domain protein {ECO:0000313|EMBL:EGC83712.1};
DE            EC=6.3.1.2 {ECO:0000313|EMBL:EGC83712.1};
GN   ORFNames=HMPREF9246_0408 {ECO:0000313|EMBL:EGC83712.1};
OS   Anaerococcus hydrogenalis ACS-025-V-Sch4.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Anaerococcus.
OX   NCBI_TaxID=879306 {ECO:0000313|EMBL:EGC83712.1, ECO:0000313|Proteomes:UP000005277};
RN   [1] {ECO:0000313|EMBL:EGC83712.1, ECO:0000313|Proteomes:UP000005277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-025-V-Sch4 {ECO:0000313|EMBL:EGC83712.1,
RC   ECO:0000313|Proteomes:UP000005277};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01331, 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:EGC83712.1}.
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DR   EMBL; AEXN01000030; EGC83712.1; -; Genomic_DNA.
DR   RefSeq; WP_004817696.1; NZ_AEXN01000030.1.
DR   AlphaFoldDB; F0H1B7; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000005277; Unassembled WGS sequence.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006807; P:nitrogen compound metabolic 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; 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; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:EGC83712.1}.
FT   DOMAIN          154..584
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   687 AA;  79413 MW;  79E37982F590F183 CRC64;
     MNLKEFGNLA FDKKTMKENV PFPVYLKWKE AARNNDILDR ETADSIAHAM KSWALSKGAT
     SYTHWFQPLN GKTANKKTAF LNRDDKHNPI NRFSGKELIK GEPDASSFPS GGMRSTFEAR
     GYTYWDLTAN SFIEDKVLYI PSVFVSFYGE KLDKKLPLIE SMNRVSKYAS PICNLFLKDE
     KTYRVKSKVG LEQEFYLIDK EFFDKRIDLE YCGMSLVGRD PMVEKEIISH YLGAIPQRVN
     DFFEDVNEQL YDLGIYMEAE HNEVGPNQFE IAIMFENANI SVDNNQLLMH ILEKTAIKHN
     LYCLLKEKPF KNMAGSGKHN NYSLATNYGK NCFSPGKDPK NNHLFLLFLS AMIKVCNKYQ
     NLIRLSSSSV SNDYRLGGNE APPSIISVFI GKDLENILKS IANDEEIKDI NNKVKIPHLG
     EIVTDSSDRN RTSPIAFTGN KFEFRMLGSS KSAADLNTVI NLSMARVLKE FYQRLEGKDD
     RDLKDEVYKI VKETYKENSR ILFQGDGYSK EWIKEAEKRG LDNHKTFLDA LVFAKKNSSY
     DLYKDEKIFS QKEIDSIINV EFEEITKFCQ QELEVLSNMI YQEILPSAMK EIKEIKSYLS
     FLDNEKLKEK AERINKNVEI LLAYGDKIKE ILKDLDKIKS QEEKAVFIQE KTRKITDQIR
     EIADKLENEI SRENYSMPRY VDMLKSL
//
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