ID A0A160DUI2_9GAMM Unreviewed; 1488 AA.
AC A0A160DUI2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glutamate synthase, large chain {ECO:0000313|EMBL:ANB18138.1};
GN ORFNames=I596_2119 {ECO:0000313|EMBL:ANB18138.1};
OS Dokdonella koreensis DS-123.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dokdonella.
OX NCBI_TaxID=1300342 {ECO:0000313|EMBL:ANB18138.1, ECO:0000313|Proteomes:UP000076830};
RN [1] {ECO:0000313|EMBL:ANB18138.1, ECO:0000313|Proteomes:UP000076830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-123 {ECO:0000313|EMBL:ANB18138.1,
RC ECO:0000313|Proteomes:UP000076830};
RA Kim J.F., Lee H., Kwak M.-J.;
RT "Complete genome sequence of Dokdonella koreensis DS-123T.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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DR EMBL; CP015249; ANB18138.1; -; Genomic_DNA.
DR RefSeq; WP_067647144.1; NZ_CP015249.1.
DR STRING; 1300342.I596_2119; -.
DR KEGG; dko:I596_2119; -.
DR PATRIC; fig|1300342.3.peg.2071; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000076830; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF133; GLUTAMATE SYNTHASE (NADH); 1.
DR Pfam; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076830}.
FT DOMAIN 19..408
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1488 AA; 159455 MW; DFED4C82470C07E2 CRC64;
MTRVRSSGLY DPAYDHDSCG FGLVANVEGR ASRWLVEQGY AALAKMAHRG GVNGDGITGD
GSGILIHRPT AWLRALAAEA GIAPAARFAA GLVFLDRDPE RATAACACLD ACLAAEGLVV
AGWREVPVAD APCGPLGLAH RPRIRQVFAD APASFDEARF ERALFRARRR AEAALADDAT
FYVVSLSAAT IGYKAMAAPG RLEEVFPDLQ RPDLAASCVV FHQRFSTNTM PNWKLAQPFR
LLAHNGEINT IRANRSWAGA RQARLRSALV DFSDLGPLVS SDGSDSQSLD NMLEVLLAGG
IDLLAAMRIL VPPAWNASDS IDEDLEAFYE YYALHSEPWD GPAGLVMCDG RYAACTLDRN
GLRPARWTLA DDGHLIVASE TGLWDLPERR VVAKGRIGPG QMLAVDLTEH RLLDNAAIDA
VNRTRAPFKQ WLRESVTYLE SYLIDPALAA EPFPPEMLAR FQKQFALTRE ERDVVLKTLA
EDEAEATGSM GDDTPAAVLS QKSRPLYEYF RQAFAQVTNP PIDPLRERLV MSLVTQIGLE
RNIFDPSPEN ARQVLLNSPV LSQRKLRQIL ALPQVADHHV KLDLYYDERI GLEAALKQLC
ADAEAAVRGG AVLVLLSDRY PAPGLLPVHA LLATGAVHAH LIDRQLRCDC NLLVETGTAR
DAHHFACLIG FGATAVYPYL AYQTLFDMNR RGELRGLEGE APSEIGRSYR RGIRKGLLKI
LSKMGISTIA GYRGAQLFEI VGLDREVVDL CFPGAPSRIG GAGFADIEAE YRVQLAAARD
PNYALPPGGL LKAVPDGEYH MYNPAVVGNL QAAVRSGDAE LYRRYADAVN GRPPSALRDL
LAFREDLTAL PDGEDVEPSD RILKRFDSAG MSLGALSPEA HEALAIAMNR LGARSNSGEG
GEDPARYGTE RMSKIKQVAS GRFGVTPAYL VNAEVLQIKI AQGAKPGEGG QLPGHKVNPL
IARLRYAKPG IGLISPPPHH DIYSIEDLAE LIHDLREVNP RALVSVKLVS HAGVGTIAAG
VVKAGADLVT VSGHDGGTGA SPLTSIRYAG VPWELGLAET HQTLVVNGLR ERVIVQTDGG
LKTGLDVVKA AILGADSFGF GTGPMVALGC KFLRICHLNS CATGVATQNE VLRRKHFLGA
PEMVENFFRF VADDVRAILA AIGAHSLGEI VGRTELLRQI DGVTAKQRRL DLSPLLARSA
LAESMQGACA AGPLVPGPGD LVEAIARDAA AAVAARSGTR LRYAVGNTDR AVGARLSGEV
ARTWGDAGMA DAPVVVELDG AAGQSFGAWN AGGVHLVLHG EANDGVGKGM AGGRIVVRPP
ADVRYATQEA SIIGNTCLYG ATGGELYAAG RAGERFAVRN SGAIAVVEGV GDHGCEYMTG
GTVVVLGRTG LNFGAGMTGG IAYVLDLERD FVDRYNHELI DIVRISLEGM ENHMQHVRNL
IRAHAQATDS VWAGRLLEDF RNMLHKVWLV KPKAASLDAL AEELRRAA
//
