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
//