ID   A0A1H3JEB9_9RHOB        Unreviewed;      1512 AA.
AC   A0A1H3JEB9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Glutamate synthase (NADPH) large subunit {ECO:0000313|EMBL:SDY37929.1};
GN   ORFNames=SAMN05444004_101293 {ECO:0000313|EMBL:SDY37929.1};
OS   Jannaschia faecimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=1244108 {ECO:0000313|EMBL:SDY37929.1, ECO:0000313|Proteomes:UP000198914};
RN   [1] {ECO:0000313|EMBL:SDY37929.1, ECO:0000313|Proteomes:UP000198914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100420 {ECO:0000313|EMBL:SDY37929.1,
RC   ECO:0000313|Proteomes:UP000198914};
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; FNPX01000001; SDY37929.1; -; Genomic_DNA.
DR   STRING; 1244108.SAMN05444004_101293; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000198914; 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..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;  164365 MW;  158C1C2B81DFCF55 CRC64;
     MTHYFSDWER DELTRRQAMD SNSLYHEDSE HASCGVGLVV NISGKRSRKV VEAGIAALKA
     IWHRGAVDAD GKTGDGAGIH VQIPVEFFKD QIRRTGHEPH EGKRIAVGQV FLPRDNFSAQ
     EVCRTIVETE VLRMGYYIYG WRHVPVNIDC LGEKANATRP EIEQILISNV KGVDEDTFER
     ELYVIRRRIE KAAIAAQISG LYLASLSCRG VIYKGMMLAE QVAEFYPDLQ DERFESAFAI
     YHQRYSTNTF PQWWLAQPFR MLAHNGEINT LKGNVNWMKS HEIRMASGAF GEMAEDIKPI
     VPKGASDSAA LDSVFEVMVR AGRSAPMAKT MLVPESWSQS AVELPDAWRD MYAYCNAVME
     PWDGPAALAM TDGRWVCAGL DRNGLRPMRY TLTGDGLLIA GSEAGMVPVD ESIVVEKGAL
     GPGQMIAVDM EKGTLFHDTE IKDKLARALP FGEWVEKITD LTEVTKGVAE TAVHSGDELR
     TRQVAAGYSI EELEQILAPM AEDGKETLAS MGDDTPSAVL SEKYRPLSHF FRQAFSQVTN
     PPIDSLREFR VMSLKTRFGN LKNVLDEDSS QTEILELPSP FVGNSQFQAM FDHFAESVVT
     IDCTFEAGGI FGALKEGLER IRAEAEDAVR SGAGHIVLTD RMQGEDKVAM PMILATSAVH
     SWLISKGLRT FCSINVRSAE CIDPHYFAVL IGCGATTVNA YLAQDSLADR IEKGLLDCTL
     DVAVDRYRQA IDAGLLKIMA KMGISVISSY RGGLNFEAVG LSRAMCAEYF PGMLSRISGI
     GTNGIQKKLE AVHASAYHGA SNVLPIGGFY KARRSGEKHA WEAKTMHMLQ TACDRGSYEV
     WKQFSHAMQS NPPIHLRDLL AIKPKGAPIP IEEVESITSI RKRFVTPGMS LGALSPEAHK
     LLNVAMNRIG AKSDSGEGGE DPAHFVPEPN GDNPSAKIKQ VASGRFGVTA EYLNHCEELE
     IKVAQGAKPG EGGQLPGMKV TDLIARLRHS TKGVTLISPP PHHDIYSIED LAQLIYDLKQ
     INPRCKVTVK LVASSGVGTI AAGVAKAKAD VILISGHNGG TGASPATSIK YAGLPWEMGL
     TEAHQVLAMN KLRERVTLRT DGGLRTGRDI VMAAMMGAEE YGIGTAALIS MGCIMVRQCQ
     SNTCPVGVCT QNPELRAKFT GTADKVVNLI TFYAQEVREI LAEIGARSLD EVIGRADLLT
     QVSRGSAHLD DLDLNPLLIT VDGADRINYD RNKPRNAVPD TLDAQIVQDA QRFLNDGEKM
     QLQYAVQNTH RTVGTRISSH VVSKFGMRNS LQPDHLTVKL QGSAGQSLGA FLAPGLKLEV
     SGDANDYVGK GLSGGTIVVR PTMASPLKAD ENTIIGNTVL YGATDGYLFA AGRAGERFAV
     RNSGASVVIE GCGSNGCEYM TGGVAVILGS IGANFGAGMT GGMAYLYDPD GSSAVLMNME
     TLVTCPVTVP HWEAQLHRLV ERHAAETNSV KARRILSDWE REKAHFLQVC PKEMLVHIPA
     PLSKNAGAIP AE
//