ID A0A1Y6FZ53_9BACI Unreviewed; 1516 AA.
AC A0A1Y6FZ53;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glutamate synthase (NADPH) large subunit {ECO:0000313|EMBL:SMQ81128.1};
GN ORFNames=SAMN05444673_4149 {ECO:0000313|EMBL:SMQ81128.1};
OS Bacillus sp. OV166.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1882763 {ECO:0000313|EMBL:SMQ81128.1, ECO:0000313|Proteomes:UP000194454};
RN [1] {ECO:0000313|EMBL:SMQ81128.1, ECO:0000313|Proteomes:UP000194454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV166 {ECO:0000313|EMBL:SMQ81128.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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; FXWM01000001; SMQ81128.1; -; Genomic_DNA.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000194454; 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 22..415
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1516 AA; 167554 MW; 0BD96CEF793DF610 CRC64;
MTYHQLPKAQ GLYRPEYEHD ACGIGLYAHI KGYATHEIVK KGLSMLCKLD HRGGQGSDPF
TGDGAGLMVQ IPDSFFRKAL QNVQLPEKGR YGVGMLFFSN NDSERENIES YINKMIEQEG
QTVLGWRTVP VNAETIGETA KQSRPFIRQV FIGANEGLLD ELSFESKLYI IRKQSEQWAM
ASDLRFYFAS LSSRTIVYKG LLTPEQVDRF YLDLQDESFV SAFALVHSRF STNTFPSWER
AHPNRYLIHN GEINTLRGNV HWMKAREKQF VSEAFGEDLQ KVLPILDTDG SDSSILDNAL
EFLVLAGRKP AHAAMMLIPE PWSENPHMTK EKRAFYEYHS CLMEPWDGPT AISFTDGKQI
GAILDRNGLR PARYYVTDDD YIIFSSEVGV IDVEPEKVIY KERLSPGKML LIDLEEGRII
SDEEVKSEMA EALPYQQWLD EQLVRLNDDG QNGEEVLSDL LVRQKSFGYT YEDISKYLVP
VVSEGKDPIG AMGNDMPLAV LSDRAQSLFN YFKQLFAQVT NPPIDSLREE IVTSTMTLLG
AEGNILNPSE LNCRRIQLDT PVITNSQLEQ LKSLDLVDFK SKVIDILFTE NIEGSLDRIC
READDAISEG VSLLILSDRN MNQKEAAIPS LLAASALHQH LIREGSRTKA SIIIESGEVR
EVHHLAALIG YGVDAINPYL AFATYKQAIL DGSLPFTYEE AVSKYVKGMT EGVVKVMSKM
GISTVQSYRG AQIFEAVGIS GDVIERYFTG TVSQLGGISL DTIAEEAKML HTAAFADSYD
HTLDSGSNFQ WRKTGEHHAF NPGTIHTLQW ACRKGDYELY KKYSKLANEE RIGFLRNLFL
FDESRTSLPI EEVETVDSIV RRFKTGAMSF GSISKEAHET LAIAMNRLGG KSNSGEGGED
SSRFILDGNG DNRRSAVKQI ASGRFGVKSH YLVNADELQI KMAQGAKPGE GGQLPGNKVY
PWVADVRGST PGVGLISPPP HHDIYSIEDL AQLIHDLKNA NRDARISVKL VSKGGVGTIA
AGVAKGAADV IVISGYDGGT GASPKTSIQH TGLPWELGLA EAHQTLMLNG LRERVVLETD
GKLMTGKDVV MAALFGAEEF GFATAPLVVL GCVMMRVCHL DTCPVGIATQ NPELRKKFTG
EADYIVNYMR FVAQEVRELM AELGFRTVDE MVGRTDVLKM SDRAKAHWKA KDLDLTPLLH
QPEGVRTFKT PQNHKIDDSL DIQKILPAVQ QALKDRIPVD ASFPITNVNR VVGTIVGSEV
SKRYGEEGLP ENTITLRFTG SAGQSFGAFV PRGVTLEISG DVNDFLGKGL SGGKLIVKTD
ESSKLSAGEN VIAGNVALYG ATSGEAYING RAGERFAVRN SGVNVVVEGI GDHGCEYMTG
GRVVILGDVG KNFAAGMSGG IAYVLADDQD AFKKLCNQEM IEIETLTKND ANELKQMIQN
HFYYTNSVKA GCVLENWENH VRKFNMVIPK DYKRMLDQIQ KQKEKGLTED EAIMSAFLAN
SSKQKNTPKQ PEAVLR
//
