ID A0A1G8S8M4_9RHOB Unreviewed; 1513 AA.
AC A0A1G8S8M4;
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:SDJ25562.1};
GN ORFNames=SAMN04487993_102355 {ECO:0000313|EMBL:SDJ25562.1};
OS Salipiger marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=555512 {ECO:0000313|EMBL:SDJ25562.1, ECO:0000313|Proteomes:UP000199093};
RN [1] {ECO:0000313|EMBL:SDJ25562.1, ECO:0000313|Proteomes:UP000199093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26424 {ECO:0000313|EMBL:SDJ25562.1,
RC ECO:0000313|Proteomes:UP000199093};
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; FNEJ01000023; SDJ25562.1; -; Genomic_DNA.
DR STRING; 555512.SAMN04487993_102355; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000199093; 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:UP000199093}.
FT DOMAIN 34..431
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 913..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1513 AA; 164489 MW; B4D6996055AA6DB3 CRC64;
MTTFDANWAA AEETKRKWME ENSLFRDEHE HSSCGVGLVV SIDGKPSRKV VEAGITALKA
IWHRGAVDAD GKTGDGAGIH VQIPVSFFYD QIDRTGHAPR KDELMAVGQV FLPRTDFAAQ
ETCRTIVETE VLRMGHYIYG WRHVPVNVDC LGEKANATRP EIEQILISNA KGIDEETFER
ELYVIRRRIE KAATAAGING LYIASLSCRS IIYKGMMLAE QVAVFYPDLM DARFESAFAI
YHQRYSTNTF PQWWLAQPFR MLAHNGEINT IKGNTNWMKS HEIRMASATF GEMAEDIKPI
IASGASDSAA LDAVFEVLVR AGRNAPMAKT MLIPEAWSKQ AVELPQAWLD MYSYVNSVME
PWDGPAALAM TDGRWVCGGL DRNGLRPMRY VVTGDGLLIA GSEAGMVPVD EGSVREKGAL
GPGQMIAVDM EEGKLYHDTE IKDRLAASQP FGEWVGKIVE LDDVLGKVSE KPLFAGSELR
RRQIAAGYTI EELEQALAPM AEDGKEMLAS MGDDTPSAVL SKKYRPLSHF FRQNFSQVTN
PPIDSLREFR VMSLKTRFGN LKNVLDESSS QTEILVLDSP FVANTQFDEL VKHFNAGLVE
IDCTFPANGG EGALRDGLAR IRAEAEDAVR SGGGHIVLTD HHQSEDKVAM PMILATSAVH
SWLTKKGLRT FCSLGVRSAE CIDPHYFAVL VGCGATIVNP YLAEDSLADR IDRGLLDGSL
TDNVARYREA IDAGLLKIMS KMGISVISSY RGGLNFEAVG LSRAMVAEYF PGMLSRISGI
GVHGIQQKAE EVHGLGFRGG RDVLPIGGFY KARKSGETHA WGAQNMHLLQ AACNKASYEL
WKTYSKAMRA NPPIHLRDLL DFKPLAEPVP LEEVESITSI RKRFVTPGMS LGALSPEAHK
TLNVAMNRIG AKSDSGEGGE DPAHFVPEPN GDNPSAKIKQ VASGRFGVTA EYLNHCEELE
IKVAQGAKPG EGGQLPGMKV TKLIARLRHS TEGVTLISPP PHHDIYSIED LAQLIYDLKQ
INPRCKVTVK LVASSGVGTI AAGVAKAKAD IILISGHNGG TGASPATSIK HAGLPWEMGL
TEAHQVLAMN KLRDRVTLRT DGGLRTGRDI VMAAMLGAEE YGIGTAALIA MGCIMVRQCQ
SNTCPVGVCT QDESLRAKFT GNAEKVVNLI TFYATEVREI LASIGARSLN DVIGRADLLR
QVSRGAEHLD DLDLNPLLIR VDGADDIVYN RDKPRNMVPD TLDAEIVRDA ARFLEDGEKM
QLSYAVQNTH RTVGTRTSSH IVRKFGMRNA LQPDHLHVKL TGSAGQSLGA FAAPGLKIEV
SGDANDYVAK GLSGGTVVVR PPMMSPLKAE DNTIIGNTVL YGATDGYLFA AGKAGERFAV
RNSGAKVVVE GCGSNGCEYM TGGVAVILGP IGANFGAGMT GGMAYLYDPE GMAGDLMNME
SLVTCPVTVD HWEAELRGLI ERHLRETGSR RAQDILQHWD SERGHFLQVC PKEMLNKITH
PLGFEQDVAV PAE
//
