ID A0A1N7LCZ5_9RHOB Unreviewed; 1512 AA.
AC A0A1N7LCZ5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glutamate synthase (NADPH) large subunit {ECO:0000313|EMBL:SIS71689.1};
GN ORFNames=SAMN05421580_10410 {ECO:0000313|EMBL:SIS71689.1};
OS Rhodobacter aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=453582 {ECO:0000313|EMBL:SIS71689.1, ECO:0000313|Proteomes:UP000186221};
RN [1] {ECO:0000313|Proteomes:UP000186221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19945 {ECO:0000313|Proteomes:UP000186221};
RA Varghese N., Submissions S.;
RL Submitted (JAN-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; FTOG01000004; SIS71689.1; -; Genomic_DNA.
DR RefSeq; WP_076484286.1; NZ_QAXT01000005.1.
DR STRING; 453582.SAMN05421580_10410; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000186221; 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:UP000186221}.
FT DOMAIN 34..431
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 912..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1512 AA; 164687 MW; 574ECD6F44D4CE38 CRC64;
MMNYDEAWVA AEEAKRKWMD EHSLYKSEDE HSSCGVGLVV ALDGKASRKV VASGIDALKA
IWHRGAVDAD GKTGDGAGIH VQIPAPYFYD QIRRTGHEPD REKLVAVGQV FLPRTDFGAQ
EACRTIVETE VLRMGHYIYG WRHVPVNTSV LGEKANATRP EIEQILIRCE KDIDDEQFER
ELYIIRRRIE KAAVTAQING LYICSLSCRS IIYKGMMLAE QVAEFYPDLK DERFTSAFAI
YHQRYSTNTF PQWWLAQPFR MLAHNGEINT IKGNINWMKS HEIRMASNAF GDAAEDIKPI
IPAGASDSGA FDAVFELMVR SGRSAPMTKT MLVPEAWSKS ASDMPQAWQD MYAYCNAVME
PWDGPAALAM TDGRWVCGGL DRNGLRPMRY VVTGDGMLIA GSEAGMVPVD EMTVREKGAL
GPGQMIAVDM REGKLYHDRD IKDRLANSQP FGEWVGKVVE LNAILRDVPE KALHTGADLR
KRQIAAGYSV EELENILSPM AEDGKEAVAS MGDDTPPAVL SKQYRPLSHF FRQNFSQVTN
PPIDSLRESR VMSLKTRFGN LKNVLEENAT QTEIWSLESP FVANAEFGEM MKAFGTTVTA
IDCTFAAGAG QDALRAGLER IRAEAEDAVR SGASHLVLTD EHQGTDKVAM PMILATSAVH
SWLTKKGLRT FTSINIRSAE CVDSHYFAVL IGAGATTVNA YLAQDSIADR IERGLLDGSL
EDNLRRYRDA IDAGLLKIMS KMGISIISSY RGGLNFEAVG LSRAMVAEYF PGMQSRISGM
GLYGIQRKLE EVHAKGWLGG QDVLPIGGFY KARKTGETHA WGAQSMHMLQ AACDRSSYDM
WKQYSAMMRA NPPIHIRDML DIKPLGKPVP IEEVESITAI RKRFVTPGMS LGALSPEAHK
LLNVAMNRIG AKSDSGEGGE DPAHFVPEPN GDNPSAKVKQ VASGRFGVTA EYLNACEELE
IKVAQGAKPG EGGQLPGMKV TELIARLRHS TKGVTLISPP PHHDIYSIED LAQLIYDLKQ
INPRAKVTVK LVASSGVGTI AAGVAKAKAD IILISGHNGG TGASPATSVK YAGLPWEMGL
TEAHQVLAMN NLRERVTLRT DGGLRTGRDI VMAAMMGAEE YGIGTAALIA MGCIMVRQCQ
SNTCPVGVCT QDPKLRAKFT GTADKVVNLI TFYAQEVREI MASIGARSLD EIIGRADLLT
QVSRGSAHLD DLDLNPLLIT VDGWDKIVYD RSKPRNYVPD TLDAEIIKDG HRFFEDGEKM
QLSYAVRNTL RTIGTRASSH IVKNFGMRNA LQPDHLTVKL TGSCGQSLGA FAAPGLKIEV
SGDANDYVGK GLSGGTIVVR PPMASPLVAA ENTIVGNTVL YGATDGFLFA AGRAGERFAV
RNSGAKVVVE GCGSNGCEYM TGGVAVILGS IGANFGAGMT GGMAYLYDPD SVAEDYMNLE
SLVTCAVTHP HWEAQLKGLI ERHVKETGSA KGLALLTDWE TEKKNFLQVC PKEMLMHLPF
PLSDEPKAVP AE
//
