ID A0A0Q4R402_9GAMM Unreviewed; 1484 AA.
AC A0A0Q4R402;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KQO01476.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:KQO01476.1};
GN Name=gltB {ECO:0000313|EMBL:KQO01476.1};
GN ORFNames=ASF01_17515 {ECO:0000313|EMBL:KQO01476.1};
OS Stenotrophomonas sp. Leaf70.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=1736233 {ECO:0000313|EMBL:KQO01476.1, ECO:0000313|Proteomes:UP000051583};
RN [1] {ECO:0000313|EMBL:KQO01476.1, ECO:0000313|Proteomes:UP000051583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf70 {ECO:0000313|EMBL:KQO01476.1,
RC ECO:0000313|Proteomes:UP000051583};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO01476.1, ECO:0000313|Proteomes:UP000051583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf70 {ECO:0000313|EMBL:KQO01476.1,
RC ECO:0000313|Proteomes:UP000051583};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KQO01476.1}.
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DR EMBL; LMLT01000003; KQO01476.1; -; Genomic_DNA.
DR RefSeq; WP_055765633.1; NZ_LMLT01000003.1.
DR Proteomes; UP000051583; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:KQO01476.1}.
FT DOMAIN 19..408
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1484 AA; 162254 MW; 7FB60D993E863016 CRC64;
MTLRNRQGLY DPQDERDACG FGMVAQLDDQ PSRLLVDTAI AALSRMTHRG GVAADGLTGD
GCGLLLRRPT VFLRRLAEEA GLRIGPNFAA GVVFLPHDAD AAQRCRDELD ARLREAGCQP
RGWRVVPTDA SVCGELARAT LPRIEQVFVD ADPSQDAAQF ALALFLARRR SEQALRETAD
YYVTTLSAEA ISYKGMVLPD KLGTFYPDLQ RHDLASSVVV FHQRFSTNTM PRWPLAHPFR
LLAHNGEINT IEGNRHWAQA RSKVWKTPRF DIAEFDPVIS MHGSDSQSMD NMLELMVAGG
MELIQALRIL VPPATQSLEF KDADLAAFYE FHGLNSEPWD GPAGIVACDG RYAACTLDRN
GLRPARWMLT SDRHFLVASE AGVWEVPTER VVQKGKLGPG QMMAIDLRRG DLLDSDAIDR
INRARAPYKQ WLHQGVTWLQ TELIDPSLAE EPFDEATLRS YHKLFQLTSE EVEQVLRPLA
ETGQEATGSM GDDTPIAVLS RQTRPLYDYF RQAFAQVTNP PIDPLREECA MSLTTQLGKE
TNIFHAGPET VNHVILNSPV LSQRKLRQLL KMEQYVERNR LIDLSYSVEE GLKAGIERIC
AQCEQAAREG VVMLLLSDRY PVPERPMVHA LLATSAVHHH LSKSGLRCDV NLIIETGTAR
DAHHMACLLG FGATAVYPYL AYQTLFDMGR RGILLLKKGG EVSQIGRSYR KGIYKGLSKI
ISKMGICTVA SYRGAQLFEI IGLDPDVVRL CFPDATARIG GVGLPRLDTE ARELAARAWN
ELAPAEVGGL LKYVHDGEYH MYNPDVVLTL QRAARTGKAE DWRAYRDAVH SRPVSALRDL
LQLRPAATPV PLDEVEPAEA LFRRFDTAAI SLGALSPEAH EALAIAMNRL GGRSNSGEGG
EDPARYGTEK RSKIKQVASG RFGVTAEYLV NAEVLQIKVA QGAKPGEGGQ LPGHKVNELI
ARLRYAKPGI GLISPPPHHD IYSIEDLAQL IHDLKQVNPD ALVSVKLVSH AGVGTIAAGV
VKAGADLITV SGHDGGTGAS PISSIRYAGV PWELGVAESH QALVGNDLRG RTLLQTDGGL
KTGLDVVKAA LLGADSFGFG TGPMIVLGCK YLRICHLNNC ATGVATQDER LREGYFTGLP
ERVENFFRLL AEEVREWLSY LGARSLDEIV GRTDLLEQLD VSPREGVKVD LSRLLAPAQY
EGSHCAAQRL YQSPDSLVTQ MDDLLADAIA HKRGGEHRFL IHNTDRSVGT RLAGTIARAH
GNHGMDDAPL SLRFRGTAGQ SFGAFNVGGL NLEVEGEAND YVGKGMAGGR LVVRPPRGAR
FEARNTAIVG NTCLYGATGG ELFAAGRAGE RFGVRNSGAL AVIEGAGDHC CEYMTDGIVA
VLGKVGLNFG AGFTGGLAYV LDIDRDFVDR YNHELIDIHR ISAEGFENYR QHLHTLVGRH
RELTGSIWAQ QILDEFRDYV GKFWLVKPKA ASIESLAAAL RNAA
//
