ID A4EX50_9RHOB Unreviewed; 450 AA.
AC A4EX50;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Gamma-glutamylisopropylamide synthetase, putative {ECO:0000313|EMBL:EBA15741.1};
GN ORFNames=RSK20926_13959 {ECO:0000313|EMBL:EBA15741.1};
OS Roseobacter sp. SK209-2-6.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=388739 {ECO:0000313|EMBL:EBA15741.1, ECO:0000313|Proteomes:UP000005964};
RN [1] {ECO:0000313|EMBL:EBA15741.1, ECO:0000313|Proteomes:UP000005964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK209-2-6 {ECO:0000313|EMBL:EBA15741.1,
RC ECO:0000313|Proteomes:UP000005964};
RA Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2006) 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:EBA15741.1}.
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DR EMBL; AAYC01000009; EBA15741.1; -; Genomic_DNA.
DR RefSeq; WP_008207729.1; NZ_AAYC01000009.1.
DR AlphaFoldDB; A4EX50; -.
DR eggNOG; COG0174; Bacteria.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000005964; 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; 3.10.20.70; 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 Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Reference proteome {ECO:0000313|Proteomes:UP000005964}.
FT DOMAIN 14..109
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 117..450
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 450 AA; 50147 MW; AA68491E3516291B CRC64;
MLSFDTLKDQ VVSGAVDTVL VCLVDMQGRL MGKRFHAKHF VAGAWEETHC CNYLLATDLD
MATPDGYAST SWERGYGDYV MKPDLSTLRP VPWLEGTVMV LCDVLDHHSH EEVPHSPRAI
LKRQVNRLTE MGYEAMCATE LEFFLFAKSF DEIRRSGFKD LEPISGYNED YSILQTTREE
HVMRPIRNHL WDAGLPIENS KGEAETGQEE LNIKYAAAMA TAEYHTIAKH GIKEIAEARG
HAVTFLPKWS HEKVGSSSHV HQSLWQDGKP AFYDESDALG MSALMKSYMA GLLKYAPDYT
AFMAPYINSY KRFMKGTFAP TRIIWSVDNR TAGYRLCGAG SKAIRVECRI PGSDMNPYLA
MAGMLAAGIA GIEEGLELQA PTTGDVYQGE TGMIPSTLRD AAAALKGSEM LRAAMGDDVI
DHYTRAAEVE IEDFDRVVTD YEIARGFERA
//
