ID A0A1G8R8S6_9RHOB Unreviewed; 1512 AA.
AC A0A1G8R8S6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glutamate synthase (NADPH) large subunit {ECO:0000313|EMBL:SDJ13358.1};
GN ORFNames=SAMN04488026_101290 {ECO:0000313|EMBL:SDJ13358.1};
OS Aliiruegeria lutimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Aliiruegeria.
OX NCBI_TaxID=571298 {ECO:0000313|EMBL:SDJ13358.1, ECO:0000313|Proteomes:UP000199382};
RN [1] {ECO:0000313|EMBL:SDJ13358.1, ECO:0000313|Proteomes:UP000199382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25294 {ECO:0000313|EMBL:SDJ13358.1,
RC ECO:0000313|Proteomes:UP000199382};
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; FNEK01000012; SDJ13358.1; -; Genomic_DNA.
DR STRING; 571298.SAMN04488026_101290; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000199382; 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:UP000199382}.
FT DOMAIN 34..431
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 912..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1512 AA; 165128 MW; 052FB62EB1A5C2EA CRC64;
MTTYDDTWAE AERAKREELA RNGMYREEDE HSSCGVGLVV AIDGKKSRKV VEDGINALKA
VWHRGAVDAD GKTGDGAGIH VQIPVPFFYD QIRRTGHEPD VEKLIAVGQI FLPRNDFGAQ
EACRTIVESE VLRMGYYIYG WRHVPVDISC LGEKANATRP EIEQILISNT KGVDEETFER
ELYVIRRRIE KAASTRRVPD FYVCSLSCRS IIYKGMMLAE QVAEFYPDLQ DERFESAFAI
YHQRYSTNTF PQWWLAQPFR MLAHNGEINT LKGNTNWMKS HEIRMAHATF GPMAEDIKPI
IPQGSSDSAA LDSVFEMLVR AGRSAPMAKT MLVPESWSKQ AVDLPQSWQD MYSYVNSVME
PWDGPAALAM TDGRWVVGGL DRNGLRPMRY VVTGDGLLIA GSEVGMVPTN ETNVIEKGAL
GPGQMIAVNM STSKLFHDKE LKDKLASSQP FSEWVEKVVE LDSVLAGETE KPVFTGAELR
KRQIAAGYSV EELEQILVPM AEDGKEAIAS MGDDTPSAVL SEKYRPLSHF FRQNFSQVTN
PPIDSLREYR VMSLKTRFGN LKNVLDEDSS QTEILILETP FVGNAQFEKL VVEFNAPMIE
IDCTFPAGGE QNALRDALDR IRTEAEDAVR SGAGHIVLTD HYQSDDKVPM PMILATSAVH
SWLTRKGLRT FCSLNVRSAE CVDPHYFAVL IGCGATVVNA YLAEDSLADR IERGLLDGPL
NEAMARYRAA IDAGLLKIMS KMGISVISSY RGGLNFEAVG LSRAMVAEYF PGMTSRISGI
GIVGVQRKAE MVHQQGWGGG TDILPLGGFY KARKSGETHA WGAQTMHMMQ SACNTGSFEL
WKQYSKKMQA NPPIHLRDLM NFKPLGRPVP IEEVESITSI RKRFVTPGMS LGALSPEAHK
TLNIAMNRIG AKSDSGEGGE DPAHFVPEPN GDNPSAKIKQ VASGRFGVTA EYLNHCEELE
IKVAQGAKPG EGGQLPGVKV TDLIARLRHS TKGVTLISPP PHHDIYSIED LAQLIYDLKQ
INPRAKVTVK LVASSGVGTI AAGVAKAKAD VILISGHNGG TGASPATSIK YAGLPWEMGL
TEAHQVLAMN KLRDRVTLRT DGGLRTGRDI VIAAMLGAEE YGIGTAALIA MGCIMVRQCQ
SNTCPVGVCT QDQKLRDKFT GSADKVVNLI TFYAQEVREI LAELGAKSLD EVIGRTDLLA
QVSRGNAHLD DLDLNPLLIT VDGANDIVYD LWKPRNPVPD TLDAQIVADA ARFLKDGEKM
QLSYAVQNTH RTIGTRTSSH IVQRFGMRNA LQPDHLTVKL TGSAGQSLGA FGAPGLKLEV
SGDANDYVGK GLSGATIVVR PPMNSPLKAD DNTIIGNTVL YGATDGYLFA AGRAGERFAV
RNSGAKVVIE GCGSNGCEYM TGGVAVILGS IGANFGAGMT GGMAYLYDPD GSSRELMNME
TLVTAPVTHP HWEAELRDLI ERHVAETESV KAADILQHWD LELRHFVQVC PKEMLVHIPH
PLGVEENAIP AE
//
