ID   A0A1X7NMF0_9MICO        Unreviewed;      1531 AA.
AC   A0A1X7NMF0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Glutamate synthase (NADH) large subunit {ECO:0000313|EMBL:SMH39152.1};
GN   ORFNames=SAMN06295885_1603 {ECO:0000313|EMBL:SMH39152.1};
OS   Rathayibacter oskolensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=1891671 {ECO:0000313|EMBL:SMH39152.1, ECO:0000313|Proteomes:UP000193711};
RN   [1] {ECO:0000313|Proteomes:UP000193711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2121 {ECO:0000313|Proteomes:UP000193711};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-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; FXBM01000001; SMH39152.1; -; Genomic_DNA.
DR   STRING; 1891671.SAMN06295885_1603; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000193711; 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}.
FT   DOMAIN          34..426
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1531 AA;  166484 MW;  87C61DFF75985BC1 CRC64;
     MAPAQPSPRV PAVPFLGTPA AQGMYDPSAE KDACGLAMVA TMRGTAGHDI IDLALEALRH
     LEHRGAVGSD AGTGDGAGII TQIPDDFLRA VAPFDLPVVG RYAVGNAFLP VDVFERERVK
     STIAEIAREE NLSVLGWRSV PVQPDEIGTL ARAAMPAIEQ LYVMSELTDD SGSPLASVRL
     DRLTFRLRKR VERELEVYFM SLSSRTMVYK GMVTTLQLEP FYPDLSDERF ASKLALVHSR
     YSTNTFPSWP LAQPFRMIAH NGEINTVQGN RNWMRARQSQ LKSPALGDLS PLFPIVSPGR
     SDSASFDETV ELLNLAGRSL PHAIMMMVPE AWENQAAAID QKRRAFYEYH SMLMEPWDGP
     AAIVFTDGEL VGATLDRNGL RPGRYVVTDD GLVVLASEIG VLDIDPAKIV RKGRLQPGRM
     FLVDTEQGRI VEDEEIKAQL ADSAPYEKWL DDGRINLKDL PEREHIVHTP ASVNRRQRTF
     GYTEEEVRLL LLPMAKAGAE PLGAMGSDTP VAVLSKRPRL LFDYFTQAFA QVTNPPLDSI
     REEVVTSLRL GLGPERNLLS SGAEHARQVV LDFPVIDNDE LAKIQHIAPR PLSHITTTIR
     GLYRVDAGPR AMQDRIDEMC TEADEAIAAG AQFLVLSDRD STKDLAPIPS LLMLAAVHHH
     LIRTENRMRV GLVVEAGDVR EVHHVATLIG YGASAVNPYL AMETCEDLVR SGMLSDISPE
     KAVKNVIKAL GKGVLKIMSK MGISTVSSYA GAQTFEAVGL SQQFVDQYFT GTVSKLGGIG
     IDVVAEENAA RHRAAYPEDG AVIAHERLAV GGEYQWRRDG APHLFNPDTV FRLQHSTRNR
     RYDVFREYTK MVDDQSTSLM TLRGMFALDT AGRTPIPIDE VEPVEAIVKR FSTGAMSYGS
     ISPEAHETLA IAMNRLGGKS NTGEGGEDTE RLLDPERRSA IKQVASGRFG VTSMYLTHAD
     DIQIKLAQGA KPGEGGQLPP TKVYPWIART RHATAGVGLI SPPPHHDIYS IEDLKQLIFD
     LKRANPSARI HAKLVSQSGI GAVAAGTAKA LADVILVSGH DGGTGASPVN SLKHAGTPWE
     LGLAETQQTL MLNGMRDRVV VQVDGQMKTG RDVVIGALLG AEEFGFATAP LIVEGCIMMR
     VCHLDTCPVG VATQNPELRK RFSGKPEFVV NFFEFIAQEV REYLSQLGFR SIDEIVGHRE
     LLDVNQAIEH WKASGLDLTP ILVGPVFSAE EPRRHGRAQQ HELEHHFDNE LIRRAANVLD
     HRGTVVIERE IRNTERAVGT MLGHEVTVRY GENGLPADSI TVILRGSAGQ SLGAFLPAGI
     TLRLEGDSND YVGKGLSGGQ IVVRPDRLST FDASANVIAG NVIGYGATQG TMFIRGMVGE
     RFLVRNSGAT AVVEGVGDHA LEYMTGGLAV ILGATGRNLG AGMSGGTAYI HDLQRELVNR
     DALASGELTL SELGSADVEI LRDLLERHVA ETESTLAQGM LDDFDGTVSR FVKVLPRDFA
     AVLATRASAL EEGLDPDGEV VWGRILEVTG G
//