ID B6GAW7_9ACTN Unreviewed; 720 AA.
AC B6GAW7;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 08-NOV-2023, entry version 44.
DE SubName: Full=Glutamate--ammonia ligase, catalytic domain protein {ECO:0000313|EMBL:EEA90643.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:EEA90643.1};
GN Name=glnA {ECO:0000313|EMBL:EEA90643.1};
GN ORFNames=COLSTE_01217 {ECO:0000313|EMBL:EEA90643.1};
OS Collinsella stercoris DSM 13279.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Collinsella.
OX NCBI_TaxID=445975 {ECO:0000313|EMBL:EEA90643.1, ECO:0000313|Proteomes:UP000003560};
RN [1] {ECO:0000313|EMBL:EEA90643.1, ECO:0000313|Proteomes:UP000003560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90643.1,
RC ECO:0000313|Proteomes:UP000003560};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Collinsella stercoris (DSM 13279).";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEA90643.1, ECO:0000313|Proteomes:UP000003560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90643.1,
RC ECO:0000313|Proteomes:UP000003560};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2008) 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:EEA90643.1}.
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DR EMBL; ABXJ01000068; EEA90643.1; -; Genomic_DNA.
DR AlphaFoldDB; B6GAW7; -.
DR STRING; 445975.COLSTE_01217; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_11; -.
DR Proteomes; UP000003560; 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 Ligase {ECO:0000313|EMBL:EEA90643.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003560}.
FT DOMAIN 86..175
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 180..610
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 720 AA; 79457 MW; 07954FF27A4A663F CRC64;
MAYRLQSSTS TSVARSDAPR REHLMADLTD RFGTMVFSED VMKKWLPKDV YKKLAATIEE
GQPLDLDVAN AVAHAMKEWA IAHGATHYAH WFQPLSGITS EKHDSFLEPN HDGTAITKFS
GKALIKGEPD ASSFPNGGLR ATFEARGYTA WDATSPAFIK DDVLCIPTAF CSYTGEALDK
KTPLLRSMTA LDEQAKRVLA LFGKHPKRVV PSVGDEQEYF LIKKDAYRKR RDLVICGRTL
FGAAPCKGQE LEEHYFGAIR PTVSAYMKDL DNELWALGIP AKTKHNEVAP CQHELAPVYS
ELNEAVDNNL LMMEKMKLIA SRHDLVCLLH EKPFEGINGS GKHNNWSLGT ADENLLDPGD
TPLENLQFVV FLTAVIEAVD KYQDLLRASV ASCGNDHRLG ANEAPPAIMS IFLGDQLTEV
VEMLMDGETS VHATTDTLTF GTVLLPNLEQ DNTDRNRTSP FAFTGNKFEF RAVGSEANVS
DANLVLDCAV AQALRDFADA LEGTPEADFQ EAALAYCAEH LREHRRILFS GDGYSEAWEK
EAESRGLCNF RTAADALPAF VAEKNLALFQ ELGVLSEAEA VCRYEVKLEK YNKLMNIEAT
TMIREARRTY RPVITAYATK VAKGLEAIRA AGAEAAMQCE QNTLNKLCNG ITDINEAIKA
LDAVHVKAES MADGQEQANC YAHEVAPAMA DLRAAVDAME EIVAADYWPV PTYDDVLFYV
//