ID C8S109_9RHOB Unreviewed; 445 AA.
AC C8S109;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Glutamate--putrescine ligase {ECO:0000313|EMBL:EEW25450.1};
DE EC=6.3.1.11 {ECO:0000313|EMBL:EEW25450.1};
GN ORFNames=Rsw2DRAFT_1737 {ECO:0000313|EMBL:EEW25450.1};
OS Rhodobacter sp. SW2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=371731 {ECO:0000313|EMBL:EEW25450.1, ECO:0000313|Proteomes:UP000010121};
RN [1] {ECO:0000313|EMBL:EEW25450.1, ECO:0000313|Proteomes:UP000010121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SW2 {ECO:0000313|EMBL:EEW25450.1,
RC ECO:0000313|Proteomes:UP000010121};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Emerson D.;
RT "The draft genome of Rhodobacter sp. SW2.";
RL Submitted (AUG-2009) 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}.
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:EEW25450.1}.
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DR EMBL; ACYY01000009; EEW25450.1; -; Genomic_DNA.
DR RefSeq; WP_008030071.1; NZ_ACYY01000009.1.
DR AlphaFoldDB; C8S109; -.
DR STRING; 371731.Rsw2DRAFT_1737; -.
DR eggNOG; COG0174; Bacteria.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000010121; Unassembled WGS sequence.
DR GO; GO:0034024; F:glutamate-putrescine ligase activity; IEA:UniProtKB-EC.
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; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
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:EEW25450.1};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Reference proteome {ECO:0000313|Proteomes:UP000010121}.
FT DOMAIN 9..104
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 111..445
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 445 AA; 49270 MW; 2F9004C51C72878D CRC64;
MKDWLRKHPQ VRTIRVAAAD LNGQARGKRI PARFADKVVK DGTRFPFSVL NLDIWGEDID
DSPLVFEQGD ADGILRPTER GFMPMPWLEA PTALLPIWMF RENGQPYEGD PRHALRAVVD
RYKARGLTPV CAMELEFFLI DDSGKTLQVP PSPRSGKRRK AAETLSIRAL DAFDTFFTDL
YDACEAMDIP ADTSTSETGL GQFEVNLMHC DDALRAADDA WLFKMLVKGL ARRHGFAASF
MAKPYPEYSG SGLHTHFSVL DEKGDNVFDS GGPKGTAMMR HAVAGCLAAM HDATLIFAPH
ANSYDRLVPG KHAPTAISWG YENRTSAIRI PAGNPAARRI EHRVAGGDVN PYLMLAAILG
SALSGIEDQA EPAPPITGNA YAVEGLPHIP ESWEAAIDAF EQRDVLSRFL PKELIRNYVL
TKRQELHYLA ELSPEEQVEL YLDSV
//
