ID   G0EYM9_CUPNN            Unreviewed;      1597 AA.
AC   G0EYM9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Ferredoxin-dependent glutamate synthase {ECO:0000313|EMBL:AEI78675.1};
DE            EC=1.4.7.1 {ECO:0000313|EMBL:AEI78675.1};
GN   Name=gltB2 {ECO:0000313|EMBL:AEI78675.1};
GN   OrderedLocusNames=CNE_1c33720 {ECO:0000313|EMBL:AEI78675.1};
OS   Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS   / N-1) (Ralstonia eutropha).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI78675.1, ECO:0000313|Proteomes:UP000006798};
RN   [1] {ECO:0000313|EMBL:AEI78675.1, ECO:0000313|Proteomes:UP000006798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1
RC   {ECO:0000313|Proteomes:UP000006798};
RX   PubMed=21742890; DOI=10.1128/JB.05660-11;
RA   Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT   "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL   J. Bacteriol. 193:5017-5017(2011).
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; CP002877; AEI78675.1; -; Genomic_DNA.
DR   MEROPS; C44.003; -.
DR   KEGG; cnc:CNE_1c33720; -.
DR   HOGENOM; CLU_000422_8_2_4; -.
DR   Proteomes; UP000006798; Chromosome 1.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016041; F:glutamate synthase (ferredoxin) 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:AEI78675.1}.
FT   DOMAIN          39..439
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1597 AA;  174607 MW;  B3F4CADE5CE9A694 CRC64;
     MDQTKNLSAQ AQTSESSHAI DLRPQAQGMY DPSNEHDACG VGMVAHIKGK KSHEIISQGL
     KILENLDHRG AVGADALMGD GAGILIQIPD QFYRDEMAAQ GVSLPPAGEY GVGMIFLPKE
     HASRLACEQE LERTVRLEGQ VVLGWRDVPV DAKMPMSPTV RTTEPVIRQI FIGRGRDIMT
     TDALERKLYV IRKTASHAIQ ALKLKHGKEY FVPSMSARTV VYKGLLLANQ VGEYYLDLLD
     QRAVSALALV HQRFSTNTFP AWELAHPYRM VAHNGEINTV KGNVNWINAR TGAISSPVLG
     DDLPKLWPLI YPGQSDTASF DNCLELLTMA GYPLVHAMMM MIPEAWEQHT LMDDNRRAFY
     EYHAAMMEPW DGPAAICFTD GRQIGATLDR NGLRPARFYV TEDDIVVLAS EAGVLPFPES
     RIVEKWRLQP GKMFLIDMEQ GRIIDDKELK DNLANAKPYK SWIDAVRIKL DELDAKPEDV
     AAEKKPVAKL LDRQQAFGYT QEDVKFLMAP MALAGEEATG SMGNDSPLAV LSSKNKTLYH
     YFKQLFAQVT NPPIDPIREN MVMSLVSFIG PKPNLLELNN INPPMRLEVS QPVLDFKDIA
     KIRNIEHYTG GKFRSYELNI CYPKTWGKEG IEARLASLCA EAVDAVRSGF NILIVSDRRV
     DAEHVAIPAL LATSAIHHHL VEKGLRTSTG LVVETGTARE VHHFALLAGY GAEAVHPYLA
     METLAEMAQG LSGDLSPEKA VKNFVKAIGK GLFKVMSKMG ISTYMSYTGA QIFEAIGLSR
     ELVQKYFHGT PSNVEGIGIF EVAEEALRLH RDAFGDNPVL ESMLDAGGEY AFRIRGEEHM
     WTPDSVAKLQ HSVRADDGKG AYQTYKEYAN IINDQSKRHM TLRGLFEFKV DPAKAIPLEE
     VESAKEIVKR FATGAMSLGS ISTEAHTTLA LAMNRIGGKS NTGEGGEDEK RYRNELRGIP
     IKQGDTLKGL LGDGVIENDL ELRDGDSLRS KIKQVASGRF GVTAEYLASA DQIQIKMAQG
     AKPGEGGQLP GHKVSDYIGK LRYSVPGVGL ISPPPHHDIY SIEDLAQLIH DLKNVNPSSD
     ISVKLVSEVG VGTVAAGVSK AKADHVVIAG HDGGTGASPW SSIKHAGTPW ELGLAETQQT
     LLLNGLRNRI RVQADGQMKT GRDVVIGALL GADEFGFATA PLVAEGCIMM RKCHLNTCPV
     GVATQDPQLR KKFQGKPEHV VNFFFFVAEE AREIMAQLGI RKFDELIGRA DLLDTKPGIE
     HWKARGLDFS RIFHQVSLGA DVPLYHTDVQ DHGLSAEAGK ALDHVLIAKA RPAIEKGERV
     SFIQPVKNVN RTVGAMLSGV VAKQHGHEGL PDDTIHIQLQ GTAGQSFGAF LAHGITLDLV
     GDGNDYVGKG LSGGRVIVRA PHEFRGDPTR NIIVGNTVLY GAIAGEAFFN GVAGERFAVR
     NSGAVAVVEG TGDHGCEYMT GGTVVVLGGT GRNFAAGMSG GVAYVYDEDG LFDKRCNTSM
     VALEAVLASA DQEKGQPQAS WHKVDGKRVL DEVILRNLIE QHFRYTGSER AKALLADWTT
     ARRKFVKVFP TEYKRALGEM YAKEQAARDS DREAIAA
//