ID A0A1I5S2P6_9BURK Unreviewed; 1584 AA.
AC A0A1I5S2P6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glutamate synthase (NADH) large subunit {ECO:0000313|EMBL:SFP64970.1};
GN ORFNames=SAMN05443579_113150 {ECO:0000313|EMBL:SFP64970.1};
OS Variovorax sp. PDC80.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882827 {ECO:0000313|EMBL:SFP64970.1, ECO:0000313|Proteomes:UP000199369};
RN [1] {ECO:0000313|Proteomes:UP000199369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PDC80 {ECO:0000313|Proteomes:UP000199369};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOWG01000013; SFP64970.1; -; Genomic_DNA.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000199369; 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:UP000199369}.
FT DOMAIN 25..425
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1584 AA; 172754 MW; 579997C584E01092 CRC64;
MTTAAEIQHL QQHGLYSGAD EHDACGVGFV AHIKGEKSHA IVLQGLKILE NLDHRGAVGA
DKLMGDGAGI LIQLPDHLYR DEMAKQGVTL PPPGEYGVGM IFLPKEHASR QACEQEMERA
IKAEGQVLLG WRDVPVNRDM PMSPTVREKE PLLRQVFIGR GNDVIVQDAL ERKLYVIRKT
ASANIQRLKL KHSKEYYVPS MSSRTVVYKG LLLADQVGTY YLDLQDKRCV SALGLVHQRF
STNTFPEWPL AHPYRYVAHN GEINTVKGNY NWMKAREGVM SSPVLGADLQ KLYPISFAGQ
SDTATFDNCL ELLTMAGYPI SQAVMMMIPE PWEQHSTMDP RRRAFYEYHA AMLEPWDGPA
SIVFTDGRQI GATLDRNGLR PSRYCVTDDD LVIMASESGV LPVPEQKIVR KWRLQPGKMF
LIDLEQGRMI DDEEVKATLA NSKPYKQWIE NLRIKLDSVQ AEPVTAPISQ VALLDRQQAF
GYTQEDIKFL MSPMAQAGEE GIGSMGNDSP LAVLSSKNKP LYNYFKQLFA QVTNPPIDPI
REAIVMSLVS FIGPKPNLLD INQVNPPMRL EVSQPILDFA DMAKLRDIGK YTQGKFKSYV
LDITYPLAWG DEGVEAKLAS LCAEAVDAIK GGHNILIVSD RGVGPTQVAI PAVLALSAVH
QYLVREGLRT TAGLVVETGS AREVHHFAVL AGYGAEAVHP YLAMDTLAGM HADLPGALSA
EKAIYNYVKA IGKGLSKIMS KMGVSTYMSY CGAQLFEAIG LNSETVSKYF TGTASRVEGI
GVFEIAEEAI RMHKAAFGDD PVLASMLDAG GEYAWRTRGE EHMWTPDAIA KLQHSTRANN
WNTYKEYAQL INDQNRRHLT LRGLFEFKID PAKAIPVDEV ESAADIVKRF ATGAMSLGSI
STEAHSVLAV AMNRIGGKSN TGEGGEDPAR YRNELKGIPI KQGDTLRSVI GAENVEVDLP
LKDGDSLRSR IKQVASGRFG VTAEYLHSAD QIQIKMAQGA KPGEGGQLPG GKVTEYIGKQ
RYAVPGVGLI SPPPHHDIYS IEDLAQLIHD LKNTAPHASI SVKLVSEIGV GTIAAGVAKC
KSDHVVIAGH DGGTGASPWS SIKHAGSPWE IGLAETQQTL VLNRLRSRIR VQADGQMKTG
RDVAIGALLG ADEFGFATAP LVVEGCIMMR KCHLNTCPVG VATQDPVLRK KFSGKPEHVV
NYFFFVAEEV RQIMAQLGIR KFDDMIGRAD LLDMRKGIEH WKASGLDFSR LFALPNVPAD
VSRFHVENQD HGLDKALDVR LIEKSRPAID KGEKVQFIEV ARNVNRSVGA MLSGALTKVH
PQGLPDDSIR IQLEGTGGQS FGAFLARGIT LYLIGDANDY TGKGLSGGRV VVRPSLDFRG
EAVRNTIVGN TALYGATTGE AYLCGVAGER FAVRLSGATA VIEGTGDHGC EYMTGGTVAV
LGKTGRNFAA GMSGGVAFVY DEDGQFASRC NMSMVSLEKV LTSAEQTASV HRKIWHGGET
DEAQLKKLLE EHHRWTGSKR ARELLDTWAV SRTKFVKVFP NEYKRALGEL HDRKVELAST
GNNAHVGLEP HAIAAAPKTA PAAA
//