ID Q0FET4_9RHOB Unreviewed; 442 AA.
AC Q0FET4;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Glutamine synthetase III {ECO:0000313|EMBL:EAU53255.1};
GN ORFNames=OM2255_06985 {ECO:0000313|EMBL:EAU53255.1};
OS Rhodobacterales bacterium HTCC2255.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU53255.1, ECO:0000313|Proteomes:UP000009381};
RN [1] {ECO:0000313|EMBL:EAU53255.1, ECO:0000313|Proteomes:UP000009381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU53255.1,
RC ECO:0000313|Proteomes:UP000009381};
RA Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (SEP-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:EAU53255.1}.
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DR EMBL; AATR01000001; EAU53255.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0FET4; -.
DR eggNOG; COG0174; Bacteria.
DR HOGENOM; CLU_017290_1_3_5; -.
DR OrthoDB; 9807095at2; -.
DR BioCyc; RBAC367336:G1GNW-839-MONOMER; -.
DR Proteomes; UP000009381; 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 InterPro; IPR027303; Gln_synth_gly_rich_site.
DR InterPro; IPR017536; Glutamine_synthetase_typeIII.
DR NCBIfam; TIGR03105; gln_synth_III; 1.
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; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Reference proteome {ECO:0000313|Proteomes:UP000009381}.
FT DOMAIN 12..94
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 100..442
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 442 AA; 48903 MW; 8226635C5E8632F5 CRC64;
MTTDLTKFAK DNGIEYFMIS FTDLFGGQRA KLVPARAIAD MQEDGAGFAG FATWLDLTPA
HPDMLAVPDP EAAIILPWDK TIAWVPGNCV MEGQDVAQAP RNVLRKLISE AADEGMHVKT
GIEAEFFLLT PNGEQISDQY DTAAKPCYDQ QAFMRRLDVI REISDYMLEM GWGAYQNDHE
DANGQWEMNW DYDDALKTAD KHSFFKFMAK CVAEKHGYKA TFMPKPIEGL TGNGCHAHIS
VWDAPGAESK VNVFAGKGEG QTGEVGLSER GKNFLGGIMK HASALAAITN PTVNSYKRIN
APRTMSGATW APNTVTWTGN NRTHMVRVPG PGRFELRLPD GAVNPYLLQA IIIAAGLSGV
RTKADPGKRH DIDMYAEGYK ITDAPKLPLN MLDALRAYDD DTELKVAMGD EFSSAYLKMK
HQEWNDFCSH FSSWEKANTL DI
//
