ID   A0A1G5FBJ8_9FIRM        Unreviewed;      1510 AA.
AC   A0A1G5FBJ8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:SCY36606.1};
GN   ORFNames=SAMN05660668_02376 {ECO:0000313|EMBL:SCY36606.1};
OS   Pseudobutyrivibrio sp. AR14.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Pseudobutyrivibrio.
OX   NCBI_TaxID=1520804 {ECO:0000313|EMBL:SCY36606.1, ECO:0000313|Proteomes:UP000198746};
RN   [1] {ECO:0000313|EMBL:SCY36606.1, ECO:0000313|Proteomes:UP000198746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR14 {ECO:0000313|EMBL:SCY36606.1,
RC   ECO:0000313|Proteomes:UP000198746};
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; FMUY01000014; SCY36606.1; -; Genomic_DNA.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000198746; 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          18..409
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1510 AA;  165987 MW;  D8D48F681865CAE0 CRC64;
     MDNQQMGLYS PEFEHDNCGI GAVVSIKGIK THQTVSDALK IVENLEHRAG KDALGETGDG
     VGILLQISHK FFSKVTKEIG ISIGGERDYG VGMFFFPGEE LKRKQAMKMF EIIVEKENLQ
     FLGWRQVPTK PEILGKAAVD CMPTIYQAFI KRPANCSKGL DFDRKLYVAR RVFEQTAEDT
     YVASLSSRTI VYKGMFLVNQ LRLFFADLHD EDYESAIATV HSRFSTNTNP SWERAHPNRF
     IVHNGEINTI KGNADKMLSR EETMVSQVLE PEMSKITPVC NQAGSDSAML DNALEFLVMN
     GMPLPLAVMI TIPEPWVKNK AMDQARRDFY QYYSTMMEPW DGPASILFSD GDIMGAVLDR
     NGLRPSRYYI TNDDYLILSS EVGVLPIPES RIKLKDRLKP GKMLLVDTVE GRLIDDNELK
     ATYAARQPYG QWLDANLAHL ADIKIPNESV PKYSPEERDR LQKAFGYSYE EIKDSILPMA
     LNGGENTGAM GIDVPLAVLS ENHQPLFNYF KQLFAQVTNP PIDSIREEIV TATTIYLGTA
     GNVLEEKEEN CNMLQINNPI LTVTDLMKIK SMNVPGIHAE TVPITYYKNT SLEKAIDHLF
     VEVDRVNREG ANIIILSDRG VDENHVAIPS LLAVAAVQHH LVQTKKRTSL SVILESGEPR
     EVHHFATLLG YGASAINPYL AQETIGELIE KGQLKKDVHA AIDAYNEAVI SGIIKIASKM
     GISTVQSYQG AKIFEAIGIS SDVIDKYFTG TISRIGGITI EDIQADVEMQ HSKAFDPLGL
     SVDETLDSRG QHKMRSGAEE HLYNPATIHL LQLSTRTGDY NTFKEYTALV NKEDAVRNLR
     GLIDFKYPKK GINIDEVESV DSIVKRFKTG AMSYGSISKE AHETMAIAMN MLQGKSNSGE
     GGEEESRYTV GPDGLNRCSA IKQVASGRFG VTSRYLVSAK EIQIKMAQGA KPGEGGHLPG
     KKVYPWIAKT RLSTPGVALI SPPPHHDIYS IEDLAELIYD LKNANKDARI SVKLVSEAGV
     GTIASGVAKA GAQVILISGY DGGTGAAPKS SIHNAGLPWE LGLAEAHQTL AMNGLRNKVV
     IETDGKLMSG RDVAIACALG AEEFGFATAP LVTMGCVMMR VCNLDTCPVG VATQNPELRK
     RFAGKPEYVV NFMRFIAQEL REYMAELGCK TVDELCGRYD LLKLKDVDES KRMGKVDLSA
     VVSNPHPYEK IEYNKKNVFN FELEKTVDEK VLLKELKKAI SSGAKGEVDV QVSNVDRSLG
     TLLGAQLTRQ YGETLEEDSY VVNCHGAGGQ SFGAFVPKGL TLKLEGDSND YFGKGLSGGK
     LVVYPSKDAT YKQDENIIIG NVALYGATSG KAFINGVAGE RFAVRNSGAT AVVEGCGDHG
     CEYMTGGRVV VLGTTGKNFA AGMSGGIAYV LDEDATLYKR LNKSMVSLET VTDKYDVLEL
     KSIIAEHVAA TGSVKGKEIY DNFSDYLPKF KRIVPFDYKL MMQTIVQMEE KGLSSEQAQI
     EAFNLLMGRR
//