ID A0A1G8CQS3_9NOCA Unreviewed; 1542 AA.
AC A0A1G8CQS3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glutamate synthase (NADPH/NADH) large chain {ECO:0000313|EMBL:SDH47798.1};
GN ORFNames=SAMN05444695_10294 {ECO:0000313|EMBL:SDH47798.1};
OS Rhodococcus triatomae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=300028 {ECO:0000313|EMBL:SDH47798.1, ECO:0000313|Proteomes:UP000183263};
RN [1] {ECO:0000313|EMBL:SDH47798.1, ECO:0000313|Proteomes:UP000183263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44892 {ECO:0000313|EMBL:SDH47798.1,
RC ECO:0000313|Proteomes:UP000183263};
RA de Groot N.N.;
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; FNDN01000002; SDH47798.1; -; Genomic_DNA.
DR RefSeq; WP_072737869.1; NZ_FNDN01000002.1.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000183263; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) 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 Reference proteome {ECO:0000313|Proteomes:UP000183263}.
FT REGION 196..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1542 AA; 164726 MW; A1C9EC0E8097C711 CRC64;
MHYSRLPGRQ GLYDPGGEAD ACGVAIVCDI EGRPSHRIVA DALDALGKLA HRGAAGAEPD
SGDGAGITLA LPVDLYARVC PFPLPGVPGS HGSCGSEREH AFATGLCFLP ADASARAEAV
RRVEAIAAEE GLEVLGWREV PVDPDRAGVG AAARACAPHI GQLFVAATRP DGGYERGVAL
DRRVLALRIR AERLRGTSDH GGESHEDGES HEDGTVYFPS LSSRTIVYKG MVTPGQLAAF
YPDLRDRRTV AAIALVHSRY STNTFPSWIL AQPFRLVAHN GEINTIRGNR NRMRSREALL
ESALLPGDLA RMFPICTPGL SDSASFDEVL ELLHLAGRTL PHAVAAMVPE TWERDAAMAP
SRRDFYRFHA SVMEAWDGPA CIAFTDGTVA GAVLDRNGLR PGRWWRTADG RMILASESGV
LDVDAAEVVE KGRLEPGAMF LVDTAAGRVV PDREVKEALA AHRPYDAWSS NLVWLDTGVR
PGEVEVPADL RRRQQVFGYT DEELRVLLAP MARSGAEPVG SMGDDTPIAA LSERPRLIYD
YFVQLFAQVT NPPLDAIREE IVTSLRSVVG PESNLLDPGP HSCRQLVLDG PILDRAQVAE
ILELATARGH RHLSAVVLPT VYDVRRGAAG MREALDRLRA RAAAAPAEGH SLLVLSDRDV
SPDRAPIPAL LAVASVHHHL VRTGHRAQVS LVVETGDARE VHHVAALLGY GASAVHPYLA
TASVADLVAS GEIDGTSVAE AVDNYVRALR RGVVKVMSKM GISTLASYTA AQVFEAIGLD
HDLVDEHFTG TTSRIGGVGL DRLSADVRRR HLRAYQENPA AAVHRPLDGG GAYRYRSDGE
MHLFTPETVF LLQHATRTGR SEVFARYSAR VDELSARGGT LRGLLRFRDV DEPIPLHEVE
PASEIVRRFG TGAMSYGSLS AEAHETLAIA MNRMGARSNT GEGGEDGARL RDPERSSAVK
QVASGRFGVT SDYLVHAEDI QIKMAQGAKP GEGGQLPGFK VYPWVAQTRH STPGVGLISP
PPHHDIYSIE DLAQLIHDLK NANDRARIHV KLVSACGVGT VAAGVAKAHA DVVLISGHDG
GTGATPLTSM KHAGLPWEIG LADTQQTLVL NGLRDRIVVQ CDGGLRTARD VTVAALLGAE
EYGFATAPLV AAGCVMMRVC HLDTCPVGIA TQNPELRGRY TGRPEFVEQY FRFVAEDVRR
HLAVLGLRSL DEAVGRADLL EAADRHEDAA SRGGLDLTPL LAVPPGSGRV ARRRGAVSAR
RDLDGSLDRT LLLPAAEPAL EDALPVRIDT PIRNVHRTVG TLLGAEITRR YGARGLPDDT
VRVVLTGSAG QSFGAFLPPG LTLELIGDAN DYLAKGLSGG RVVVRPDPAA PFEAQGQVIA
GNTLLYGATS GEVFLRGRVG ERFAVRNSGA LAVVEGIGDH GCEYMTGGRV LVLGPIGRNF
AAGMSGGIGY VLDLDRSRVN LDMVEIEPVD ADDVAWLRGV LARHRERTGS VVASALLAHW
PAAADSVSKV MPVDYRRVLA ATRAAETEGL DVDSAVMEAA RG
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