ID A0A1G9R7S4_9FIRM Unreviewed; 1522 AA.
AC A0A1G9R7S4;
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 (Ferredoxin) {ECO:0000313|EMBL:SDM18485.1};
GN ORFNames=SAMN05660299_00406 {ECO:0000313|EMBL:SDM18485.1};
OS Megasphaera paucivorans.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=349095 {ECO:0000313|EMBL:SDM18485.1, ECO:0000313|Proteomes:UP000199309};
RN [1] {ECO:0000313|EMBL:SDM18485.1, ECO:0000313|Proteomes:UP000199309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16981 {ECO:0000313|EMBL:SDM18485.1,
RC ECO:0000313|Proteomes:UP000199309};
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; FNHQ01000002; SDM18485.1; -; Genomic_DNA.
DR STRING; 349095.SAMN05660299_00406; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000199309; 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:UP000199309}.
FT DOMAIN 24..422
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 910..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1522 AA; 169092 MW; 241D74B214A3C277 CRC64;
MYEKLRDLPA PQGLYDPSYE HDACGIGFVV NIKGEKTYDI IDDALSILEN LKHRGAEGAD
AKSGDGAGIL VQIPHQFFCR ECEVLGFSLP DEGEYGVGMI FTHRYENFRK KQITAFEKIV
RSEGQSILGW REVPIDESLI GSIAKNVRPR FLQVFIKKSP EIQTQMDFER KLYVIRKLAE
KEIIPESQAM GTDFYIASLS SRTIVYKGML TSLQLRHFYL DLSDLDFTTA MALVHSRFST
NTFPSWARAH PNRYIVHNGE INTIQGNINW LNARESKSQS PLFPDLEKVF PVVDDSGSDS
AMFDNCLEYL YMTGHSLPHA MMMMIPEPWE KDPLMSQEKR DFYRYHNFMM EPWDGPAAIA
FCDGVVIGGM LDRNGLRPTR YYVTKDDRVI VSSEVGTVNI DQRNILYKGR LEPGKMLLVD
TRQKRIIDDD EIKHQIASEH PYGEWYKDHI VDLDELMEGR DMADNDNLIP YDIKEQEKVF
GYTQEDMDKI ILPMARDGKH AIDSMGVDVP LAVLSEQPQP LYDYFKENFA QVTNPPIDGV
RENTVTSPIV MCGNVANIMD PNESGTAALF MKQPILTNEE MSVIKSLLTP KLRSATISML
YPVNGGPEAM ETAIESLCID ALKAIKNGAN ILILSDRGVN SRMAAIPALL ASAALHNYLI
KRTVRSDVGL ILESGEPREV HHFCALIGYG ITAINPYLAL ETIKELMQKK KLPKTDYTTA
KNNYIKASVN GILAVMSKMG ISTIHSYHGA QIFEAVGIKK DLINKYFVNT PSRIEGIGIT
EIAKENELRH ANAYEESTNN LPTGDFYMYH KGGQPHIIDP ETVQLLQKAC QTNEYGLYKE
YSHKVNDAAM FRLRDLLEFD YPTGCSIPIE EVESVDTIVK RFRTGAMSYG ALSKEAHECI
AIAMNRLGGM SNTGEGGEDP SRFERRTNGD NANDQIKQVA SARFGVTSNY LVHARELQIK
CAQGAKPGEG GHLPGSKVYP DIAKTRHATT GVSLISPPPH HDIYSIEDLA ELIFDLKNAN
RFARISVKLT SGAGIGTIAA GVVKAKADAI LVSGYDGGTG ASPRTSLRHA GLPWELGLSE
VQQTLLLNQL RDRVMLEVDG KLLTGRDVAI AALFGAELFG FGTAPLIAIG CHMLRVCHMN
TCPYGVCTQN EKLRKKFKGK PEYIINFMRF IAQDLREIMA RLGFHTISDM VGRYDRLKQK
ENIANWKAAT ISLENLLFRP YTDSSVGHHF TKPQDHNIDN TLDMSKLVRM CRPALAQQKH
IRSRLRIKNT DRVTGTLLGS EISRRYGEAG LAEDTIKLSF VGSAGQSFGA FIPKGLTLEL
EGDANDYLGK GLSGGKIIVY PPREAEFPAE DNIIIGNVAF YGATNGEAYI NGIAGERFCV
RNSGISAVVE GIGNHGCEYM TGGCVLILGK TGQNFAAGMS GGVAYVLDLE PALCNHDLVL
LKDLTDEIEQ DLVRRMLEKH VAYTGSDLGG RLLDNWIETV GRITKVIPEA YEEILGLIAQ
AEADGHTPEE AQMIAFTQKH AK
//
