ID C9MZ44_9FUSO Unreviewed; 701 AA.
AC C9MZ44;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Glutamate--ammonia ligase, catalytic domain protein {ECO:0000313|EMBL:EEX74032.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:EEX74032.1};
GN Name=glnA {ECO:0000313|EMBL:EEX74032.1};
GN ORFNames=GCWU000323_01841 {ECO:0000313|EMBL:EEX74032.1};
OS Leptotrichia hofstadii F0254.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=634994 {ECO:0000313|EMBL:EEX74032.1, ECO:0000313|Proteomes:UP000006233};
RN [1] {ECO:0000313|EMBL:EEX74032.1, ECO:0000313|Proteomes:UP000006233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0254 {ECO:0000313|EMBL:EEX74032.1,
RC ECO:0000313|Proteomes:UP000006233};
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 (SEP-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:EEX74032.1}.
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DR EMBL; ACVB02000018; EEX74032.1; -; Genomic_DNA.
DR RefSeq; WP_006805152.1; NZ_GG700633.1.
DR AlphaFoldDB; C9MZ44; -.
DR STRING; 634994.GCWU000323_01841; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_0; -.
DR Proteomes; UP000006233; 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 Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:EEX74032.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006233}.
FT DOMAIN 62..155
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 160..592
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT COILED 618..659
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 701 AA; 78697 MW; CFB3336600AEE9B9 CRC64;
MENAMKSFGE NVFRDSNLKK RVSKAVFKEF KASQLGETEL SKETAEVIAN AIKDWATKRG
ATHYCHWFQP LNDLTAEKHD SFLEPTENEE LIYKFSGKNL IKGESDASSF PNGGLRSTFE
ARGYTIWDTS SYPFIRENKN GVTLYIPTAF ISFTGEALDK KVPLLRSMKY ISGQALRVLR
AFGNKTSNHV FNTLGVEQEY FLVKKDMFEA RDDLLLTGRT LFGASAPKGQ ELSDHYYGKI
KEKVINFMSD VDVELWKLGI PSKTRHNEVA PNQFEVAPLF SVANLASDQN QIIMETIEKT
ALRHDLVALL HEKPFAGVNG SGKHNNWSLG TDDGKNLFSP GKDMKSNTQF LIFVAAVIEA
VDRYYPMLRY ATATATNDHR LGGHEAPPAI ISVFLGDELT TVLNNIAYKK DAPVSESSKV
NLSVDVLPAF SMDAGDRNRT SPFAFTGNKF EFRMPGSSST PATSAAVINA MVGKVLSEYA
DKLEKATEKS LPKVANEIIA NAYKKHHRII FNGNGYSEEW AKEAKKRGLT NEVASNTALR
KMIDKDVLEL TQEIGMLSEQ ESIARYNAYA ERYITQLSIE SRTLIDIANK NILPSGLKYA
NLLADHIEKN SKYGKAFIKE QEEILKDVLA NITNLRKEVK SLEKEINRVR NEKDLGKQTD
LAKEKLVTGL EGLRIPCDNL EKVIDQEYWS FPTYTDLLFK L
//