ID C2BH60_9FIRM Unreviewed; 686 AA.
AC C2BH60;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN Name=glnA {ECO:0000313|EMBL:EEI85703.1};
GN ORFNames=HMPREF0072_1680 {ECO:0000313|EMBL:EEI85703.1};
OS Anaerococcus lactolyticus ATCC 51172.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=525254 {ECO:0000313|EMBL:EEI85703.1, ECO:0000313|Proteomes:UP000005984};
RN [1] {ECO:0000313|EMBL:EEI85703.1, ECO:0000313|Proteomes:UP000005984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51172 {ECO:0000313|EMBL:EEI85703.1,
RC ECO:0000313|Proteomes:UP000005984};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (OCT-2008) 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:EEI85703.1}.
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DR EMBL; ABYO01000247; EEI85703.1; -; Genomic_DNA.
DR AlphaFoldDB; C2BH60; -.
DR STRING; 525254.HMPREF0072_1680; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_9; -.
DR Proteomes; UP000005984; 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:EEI85703.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005984}.
FT DOMAIN 159..583
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 686 AA; 78360 MW; 212EF4AB9D3C1292 CRC64;
MKEFGNLAFD KKTMKENVPY PVYLKWKEAA RNNATLDRET ADSIAHAMKI WAISKGATSY
THWFQPLNGK TATKKTAFLN RDDKHNPINR FSGKELIIGE PDASSFPSGG MRSTFEARGY
TYWDLTANSF ILDKVLYIPS VFVSFYGEKL DKKLPLIESM NMVSKVSSKL CNLFLKDEHT
YRVKAKVGLE QEFYLIDKKY FDQRIDLEYS GMTLVGSDPM VEKELISHYL GAIPERVNDF
YEDVNKALYD LGIYMEAEHN EVGPNQFEIA IMFENANISV DNNQLLMYIL EKTALKHDLV
CLLKEKPFKN MAGSGKHNNY SLATNYGKNL FSPGKDPKNN MIFLLFLSAM VEFCNKYQKL
IRIASSTVSN DYRLGGNEAP PAIISMFIGC DLEEVLKAIA NDDFEEKIIA NKVKIPHLGE
IKTDTSDRNR TSPIAFTGNK FEFRMLGSSQ SAADLNTVIN IGMAEALEKI YARLEGCSEE
NLKEEAYKII KEIYLANKNI LFQGDGYSED WKKEAEKRGL ENYPTYLDAL KAAKDARAYA
IFEKVGIFSQ KEIESLIYVG FEDVIKFFSA QLEILNNLIH QEILPSAMRE IKGIKDYLSF
MENEKLSQRA RRINEEVGEL LAYSEKISHL IERSEEIPDI EAKADFLQKE TRQVAGEVRK
ISDSLEKLIS RENYSMPNYV DMLKTL
//