ID A0A133ZD28_9ACTN Unreviewed; 713 AA.
AC A0A133ZD28;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE SubName: Full=Glutamate--ammonia ligase, catalytic domain protein {ECO:0000313|EMBL:KXB53337.1};
GN ORFNames=HMPREF3190_00678 {ECO:0000313|EMBL:KXB53337.1};
OS Coriobacteriales bacterium DNF00809.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales.
OX NCBI_TaxID=1588753 {ECO:0000313|EMBL:KXB53337.1, ECO:0000313|Proteomes:UP000070490};
RN [1] {ECO:0000313|Proteomes:UP000070490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00809 {ECO:0000313|Proteomes:UP000070490};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) 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:KXB53337.1}.
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DR EMBL; LSCX01000015; KXB53337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133ZD28; -.
DR STRING; 1588753.HMPREF3190_00678; -.
DR PATRIC; fig|1588753.3.peg.652; -.
DR Proteomes; UP000070490; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
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:KXB53337.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070490}.
FT DOMAIN 81..170
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 182..605
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 713 AA; 79552 MW; F5C80968427689B6 CRC64;
MLSNDIRSFY VALKERNRQM SEHLHPFGSL VFDKRTMREW LPSTTYKQLM KTIDNGEPLN
LEVAQVVAHA MKEWAIQKGA THFTHWFQPL SGVTSEKHDA FLWPQAEGGA LTRFSGSELI
QGEPDASSFP SGGLRATFEA RGYTAWDPTS YAFIKDEVLC IPTAFCSYNG EALDKKTPLL
RSMHALEKQA KRVLALFGET PQRILCTVGA EQEFFLISEK DYASREDLVL CGRTLFGAPA
CKGQELEEHY FGAIRPTVNA FMKELDDELW ALGIAAHTKH NEVAPAQHEL APVYTNANRA
IDENLLTMEK MRLLASHHGL ACLLHEKPFE GINGSGKHNN WSMSADGTNL LDPGENPRAN
LRFLVILCAI VEAVDTYQEL LRMSIASAGN DHRLGAHEAP PAIVSIFLGS ELGGIVDALI
HGKEFKTAGQ IAMDLGVEVL PRFMKDNTDR NRTSPFAFTG NKFEFRMPGS STNLSDATMV
LNTAVAKSLK TFADALEGVA PDQFEQAAIS YIKSSFTTHA NIIFNGNGYA AQWEKEAQAR
GLSNKKTAAD AFSAYVSDEA LKLFEEMEVL HETEVRSRYE VKLEKYNKLL SIECSVMERM
AQRTYIPAVD RYLGDVARRI KNMARISLKC NTDLALAKRL AKGIDAAAAA LHDLQEKHEH
AQSIEDQQER ALYYAYDVQA AMHALRSAID SLEVITSRDY WPCPSYNNLL FYV
//
