ID   A0A1I7L1W6_9BURK        Unreviewed;      1573 AA.
AC   A0A1I7L1W6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Glutamate synthase (NADPH/NADH) large chain {ECO:0000313|EMBL:SFV03701.1};
GN   ORFNames=SAMN05216552_102230 {ECO:0000313|EMBL:SFV03701.1};
OS   Pseudoduganella namucuonensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Pseudoduganella.
OX   NCBI_TaxID=1035707 {ECO:0000313|EMBL:SFV03701.1, ECO:0000313|Proteomes:UP000199391};
RN   [1] {ECO:0000313|Proteomes:UP000199391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.11014 {ECO:0000313|Proteomes:UP000199391};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FPBO01000022; SFV03701.1; -; Genomic_DNA.
DR   STRING; 1035707.SAMN05216552_102230; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000199391; Unassembled WGS sequence.
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:UP000199391}.
FT   DOMAIN          16..416
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1573 AA;  171449 MW;  563E47BF265115B5 CRC64;
     MISQGLYDPA NEHDACGVGF VAHIKGNKSH SIVEQGLLIL KNLDHRGAVG ADALMGDGAG
     ILIQIPDQYY RDEMAKQGVE LPPPGEYGVG MVFLPKENAS RIACEQEIER AVRIEGQVVL
     GWRNVPVDYD MPMSPTVRAK EPIIRQIFIG RGPDIMVTDA LERKLYVIRK SSGHAIQALK
     LIHGKEFFVP SMSARTVVYK GLLLADQVGV YYKDLQDPRC ISALAMVHQR FSTNTFPEWP
     LAHPYRLLAH NGEINTVKGN FNWMRAREGV MKSAVLDQDL QKLFPLIYEG QSDTACFDNA
     LELLLMAGYP IAQAMMMMIP EAWENHTTMD ENRRAFYEYH AAMMEPWDGP AAMAFTDGRY
     IGGTLDRNGL RPARYIVTDD DLVVMASESG VLPIPESKII QKWRLQPGKM FLIDLEAGRI
     IDDKELKDTY ANAKPYKAWI NAVRIKLNEI KLSESQLAHN RIKYSAAPGE KAVASVLDRQ
     QAFGYTQEDM RFVLAPMAVN GEEATGSMGN DSPLAVMSNK LKPLYNYFKQ LFAQVTNPPI
     DPIREAMVMS LVSFIGPKPN LLDTNNVNPP MRLEVAQPVL GFDDMARLRG ISLHTGGKFK
     SYELNICYPL AWGKEGVEAC LASLCAEAVD AVKSGHNILI VSDRSIGADR VAIPALLATS
     TIHQHLVSKG LRASTGLVVE TGSARETHHF ALLAGYGAEA VHPYLAMETL LELAPTLQGE
     LTGEKAIYNY TKAIGKGLMK VMSKMGISTY MSYCGAQIFE AIGLNKSLVD KYFKGTASNV
     EGIGVFEVAE EALRLHNLAF GNDPVLKDAL DAGGEYAFRI RGEDHLWTPD AIAKLQHSTR
     SNSYSTYKEY AQIINDQSKR HLTLRGLFEF KLDPTKAIPL EEVEPAKEIV KRFATGAMSL
     GSISTEAHAT LAVAMNRIGG KSNTGEGGED PARYSMELKG IPIKQGDTMA SVVGKEQVVV
     DIPLQAGDSM RSRIKQVASG RFGVTAEYLN SADQIQIKMA QGAKPGEGGQ LPGHKVSEYI
     AQLRFSVPGV GLISPPPHHD IYSIEDLAQL IHDLKNANPR ASISVKLVSE VGIGTVAAGV
     TKAKADHVVV AGHDGGTGAS PLSSVKHAGT PWELGLAETQ QTLVLNGLRS RIRVQADGQM
     RTGRDVVIAA MLGADEIGFA TAPLVVEGCI MMRKCHLNTC PVGVATQDPE LRAKFNGKPE
     YVVNYFFFVA EEARQLMAQL GIRTYDELIG RADLLDKKKA VTHWKASGLD FSNIFYQPEV
     AEGQAIRHVE NQDHGLEKAL DHKLIAQAKA ALEKGERVSF ISPVRNVNRT VGTMLSGEVA
     QRYGHAGLPD DTIHIQLQGT AGQSAGAFLA HGITLDLVGE GNDYVGKGLS GGRIIVRPNT
     EFRGWAVNNI IIGNTVMYGA IAGEAFFNGV AGERFAVRNS GATAIVEGTG DHGCEYMTGG
     TVVVLGATGR NFAAGMSGGI AYVYDPDGDF AQKCNLSMVS LESVVSASEQ KVDQATWHSQ
     HRNGEPEADE VILKRLIERH FKHTGSTRAR FLLDNWAEGR GKFVKVFPNE YKRALIELAE
     DAALEMETQA IAA
//