ID   A0A285LS42_9NOCA        Unreviewed;      1548 AA.
AC   A0A285LS42;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Glutamate synthase (NADH) large subunit {ECO:0000313|EMBL:SNY87273.1};
GN   ORFNames=SAMN04244553_4214 {ECO:0000313|EMBL:SNY87273.1};
OS   Nocardia amikacinitolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=756689 {ECO:0000313|EMBL:SNY87273.1, ECO:0000313|Proteomes:UP000219565};
RN   [1] {ECO:0000313|EMBL:SNY87273.1, ECO:0000313|Proteomes:UP000219565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45537 {ECO:0000313|EMBL:SNY87273.1,
RC   ECO:0000313|Proteomes:UP000219565};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OBEG01000004; SNY87273.1; -; Genomic_DNA.
DR   STRING; 1379680.GCA_001612615_03523; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000219565; 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:UP000219565}.
FT   DOMAIN          25..434
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1548 AA;  168638 MW;  2FC529EA5DAA93D4 CRC64;
     MTQLPGHRSP GPIGLYDPAN EHDACGVAFV VDMHGRRSRD IVDKAITALL NLEHRGAAGA
     EPNSGDGAGV LIQIPDRFFR AIVDFELPAE GAYASGIAFL PQARREAARA AYGVEKIVKE
     EGLEVLGWRE VPIDDSSLGA LSRDAMPTFR QIFIASPKGA AEQLSGMDLE RRAYVIRKRV
     EHELGSQGAG EGAVGKESVY FPSLSGQTFV YKGMFTTPQL RAFYLDLQDD RVESALGIVH
     SRFSTNTFPS WPLAHPFRRV AHNGEINTVT GNENWMRARE ALLNSDVFGT DSAGKNRLEK
     IFPVCTPGAS DTARFDEVLE LLHLGGRSLP HAVLMMIPEA WERNENMDPQ RRAFYEYHSM
     LMEPWDGPAS VCFSDGTVIG AVLDRNGLRP SRIWVTEDGL VVMASEVGVL DIDQSKVVKK
     ARLQPGRMFL VDTSKGRIVT DDEIKSELAA EHPYQQWLDE GVTRLADLPD RPHVHMSHDR
     VLIRQQIFGY TNEELNLLIS PMAKTGLEAL GSMGTDTPIA VLSSRPRLLF DYFSQLFAQV
     TNPPLDAIRE EVVTSLKRNI GPEADLMHPG PESCKQIAIE QPILDNDELA KLVHINDDGS
     RPELRSVVVR GLYPVKKGGK GLRKALEAIN TQVSAAIDGG ARIIVLSDRE SNEKLAPIPS
     LLLTSSVHHH LVRERTRTKV GLIVEAGDAR EVHHMAMLVG FGAAAINPYM AFETIEDMLE
     RGALDLGTGS LETDFRKAVA NFNKAAGKGV LKVMSKMGIS TLASYNGAQL FQVIGLSQDL
     VDEYFTGLRS HLGGIGLDEI ADEVAARHRV AFLENRNERA HRELEVGGEY QWRREGEYHL
     FNPDTVFKLQ HATRSGQYSI FKEYTKLVDD QSERLASLRG LFKFKSGERA PISIDEVEPA
     SEIVKRFSTG AMSYGSISAE AHETLAIAMN RLGGRSNSGE GGEHPARFEV EENGDWRRSA
     IKQVASGRFG VTAHYLTNCT DIQIKMAQGA KPGEGGQLPA HKVYPWVAEV RHSTPGVGLI
     SPPPHHDIYS IEDLAQLIHD LKNANPQARI HVKLVAEPGV GTVAAGVSKA HADVVLISGH
     DGGTGASPLT SLKHAGGPWE LGLAETQQTL LLNGLRDRIV VQVDGQMKTG RDVVIAALLG
     AEEYGFATAP LVVSGCIMMR VCHLDTCPVG VATQNPVLRE RFTGKPEFVE NFFMFIAEEV
     RELLASLGFR TLDEAIGRVD MLDTSKAKQH WKASKLDLSP ILDDVETAFM SQDRRCTKSQ
     DHGLDKALDQ QLITQSRDAL ERGKPVKFET KITNVNRTVG TMLGHEVTKL YGGTGLPDDT
     IDITFTGSAG NSFGAFVPAG ITLRVQGDAN DYVGKGLSGG HIVVRPSQNA PADFVADQNI
     IAGNVILFGA TSGKAFISGV VGERFAVRNS GATAVVEGVG DHGCEYMTGG RVVILGETGR
     NFGAGMSGGV AFVYDPEGTF AARVNPEQSD AIEQLSGDDF TWLHDIVAEH RDQTGSAVAD
     RILSDWSQQV NHFVKVMPRE YKKVLLAISE AEKSGKDVDE AIMEAARG
//