ID A0A1G4SAN4_9CAUL Unreviewed; 480 AA.
AC A0A1G4SAN4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glutamate--putrescine ligase {ECO:0000313|EMBL:SCW66282.1};
GN ORFNames=SAMN02927928_2513 {ECO:0000313|EMBL:SCW66282.1};
OS Asticcacaulis taihuensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=260084 {ECO:0000313|EMBL:SCW66282.1, ECO:0000313|Proteomes:UP000199150};
RN [1] {ECO:0000313|EMBL:SCW66282.1, ECO:0000313|Proteomes:UP000199150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3431 {ECO:0000313|EMBL:SCW66282.1,
RC ECO:0000313|Proteomes:UP000199150};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000256|ARBA:ARBA00003117}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; FMTS01000004; SCW66282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4SAN4; -.
DR STRING; 260084.SAMN02927928_2513; -.
DR Proteomes; UP000199150; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR008147; Gln_synt_N.
DR InterPro; IPR036651; Gln_synt_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF12; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE PUUA; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:SCW66282.1};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231}.
FT DOMAIN 39..134
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 141..480
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 52515 MW; 3BB6CD31B9AC6B22 CRC64;
MSTFGKSSAP AKGKSDRSLP LSERVATVEE ARAFLDANPH INYFEILFTS MTGVPRGKRL
RRHELLPIYE YGRFLPGSIL VVDTLGADCE DTGLVWEDGD ADRVARPVPG TLVPAPWLGD
DVGQVMLSLY ELDGTPNDLD PRHVLQHVLD RYKADGLTPV VACELEYYLV DIERGHDGQL
MPATGFNTGE NPKGIQVYGL PEIEAHGAFF RQLWETADAQ NIPLEGAISE FAPGQVELTL
KHKPDALRAA DDAVMYKRLA KGVALSLGIE ATFMAKPWAD RAGSGFHVHI SVADKDGNNL
CASEDPQGSK LLHNMIGGMK DHLADVMGIL APGANSYKRF KANSYAPVGL TWGVNNRTVS
LRVTAGPAHT RHVEHRVAGA DANPYLVLAA ILACAHHGIT HKTNPGPAVI GNGYAVAAES
GATLPTNWFA AVDYLDKSKV LRDYLGDRFI DMYVKVKRTE QARFFEEITE LDYDWYLRNA
//
