ID E7RLZ9_9BACT Unreviewed; 754 AA.
AC E7RLZ9;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Glutamate--ammonia ligase, catalytic domain protein {ECO:0000313|EMBL:EFZ37780.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:EFZ37780.1};
GN Name=glnA {ECO:0000313|EMBL:EFZ37780.1};
GN ORFNames=HMPREF0663_10149 {ECO:0000313|EMBL:EFZ37780.1};
OS Hoylesella oralis ATCC 33269.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=873533 {ECO:0000313|EMBL:EFZ37780.1, ECO:0000313|Proteomes:UP000005580};
RN [1] {ECO:0000313|EMBL:EFZ37780.1, ECO:0000313|Proteomes:UP000005580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33269 {ECO:0000313|EMBL:EFZ37780.1,
RC ECO:0000313|Proteomes:UP000005580};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-2011) 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:EFZ37780.1}.
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DR EMBL; AEPE02000002; EFZ37780.1; -; Genomic_DNA.
DR AlphaFoldDB; E7RLZ9; -.
DR STRING; 28134.SAMN05444288_0696; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_10; -.
DR Proteomes; UP000005580; 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:EFZ37780.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005580}.
FT DOMAIN 110..199
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 204..640
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 754 AA; 85493 MW; E3F38740714F4A14 CRC64;
MVHSRARRNR KEKNNNTLTI KEPKTMANLR FEVVAEAFRK KPLEITAPSE RPSEYFGKYV
FNRAKMYKYL PVGVYEKLTD VIDNGARLDR SIADAVAEGM KRWAEENGVT HYTHWFQPLT
EGTAEKHDAF VEHDGKGGMI EEFSGKLLVQ QEPDASSFPS GGIRNTFEAR GYSAWDPTSP
VFIIDDTLCI PTIFISYTGE ALDYKAPLLR SLHAVGKAAA EVCRYFYPDV KKVTTNLGWE
QEYFLVDESL YSARPDLMLT GRTLMGHDSA KNQQMDDHYF GTIPDRVQAF MKDLEVQALE
LGIPCKTRHN EVAPNQFELA PIFEECNLAV DHNMLLMSLM KRVARKHGFR VLLHEKPFAG
VNGSGKHNNW SLSTDTGILL HGAGKTAEDN LRFVVFIVET LMGVYRHNGL LKASIMSATN
AHRLGANEAP PAIISAFLGK HLSDLLEHIE NSHKADLFVL QGKKGMQLDI PQIPELMIDN
TDRNRTSPFA FTGNRFEFRA VGSEANCASA IIVLNAAVAE ALADFKKRVD ALIKKGEDKV
SAIVDIVRED IKTCKPIHFD GNGYSDEWIE EARRRGLDCE TSCPLVFDRY LDADSVRMFE
TANVMHRNEL EARNEVKWET YTKKIQIEAR VMGDLSMNHI IPVATHYQSR LAKNVQNMYA
IFDQAEAARL TARNVKIIKE IARRTQTIET GVEELVDARK VANKISDERA KAIAYHDTVE
PKMKEIRYQI DKLELLVADE LWTLPKYREL LFIR
//