ID A0A110BEV4_9BURK Unreviewed; 1477 AA.
AC A0A110BEV4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:AMC33165.1};
GN Name=gltB {ECO:0000313|EMBL:AMC33165.1};
GN ORFNames=VN23_00260 {ECO:0000313|EMBL:AMC33165.1};
OS Janthinobacterium sp. B9-8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1236179 {ECO:0000313|EMBL:AMC33165.1, ECO:0000313|Proteomes:UP000069577};
RN [1] {ECO:0000313|EMBL:AMC33165.1, ECO:0000313|Proteomes:UP000069577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B9-8 {ECO:0000313|EMBL:AMC33165.1,
RC ECO:0000313|Proteomes:UP000069577};
RA Xu X., Jin W., Wu Q., Jiang L., Huang H.;
RT "The whole genome sequence of Janthinbacterium sp. B9-8, a bacterium
RT isolated from low temperature sewage.";
RL Submitted (JAN-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; CP014222; AMC33165.1; -; Genomic_DNA.
DR RefSeq; WP_046350263.1; NZ_CP014222.1.
DR STRING; 1236179.VN23_00260; -.
DR KEGG; jab:VN23_00260; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000069577; Chromosome.
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 21..405
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1477 AA; 161217 MW; 76E830CB4D27BF75 CRC64;
MDRQGWLKGT LYSPTFEQDS CGFGLIAQMD DKPSHWLVST AISSLACLTH RGAVAADGKS
GDGCGLLFRK PDGFLRAVAA ENNLTVADEY AVGIVFYSAE ATLTKLFAAM EEQGLSVAGV
RSVPVNVDAC GEYALQTLPQ IGQLFVNAPA GMTSQVFERK LYQARRVAEK ANTDDVAFYM
PTLNPHVLSY KGLVTPDNLP EFYLDLKDPR FESSLAVYHQ RFSTNTWPQW KLAQPFRYLA
HNGEINTLHG NRLWAKAREA IMDSEHLDMD TVRPIVQTNG SDSMSMDNML EGLLMGGMDV
FRAFRMLVPP AWQNVDSNDR DLRAFYEYNS MHMEPWDGPA GIVWTNGRYA GCALDRNGLR
PARYVITKDR HLTIASEIGV WGYKPEDVVK KGRVKPGQIV AVDLSNGEFL DTETIDNRLK
TAQPYRAWVK KHAQHLELAE DNSPLEAMSR EQLLAYQKQF QLTFEERDQI LRVLAADGQE
AIGSMGDDTP MAVLSEKVRS PYDYLRQQFA QVTNPPIDPI REAIVMSLNT CFGPERNLFK
ETEFNASRLE VRSPVLSSDK FDSLTTMQDP DYKPAFFDIT FDPAQTTLKA AIEALRANVL
ASVRDEKTVV VVLSDKNIQK GRLPIPALFA VGAVHHELVN EGLRCLTNII VETATTRDPH
HFACLIGYGA TAVFPYLAYQ TIKELVEIGQ LDLPLEKAAN NFRKGINKGL LKILSKMGIS
TVASYRGSQL FEAVGVNEEV VDFCLNGTVS RISGANFADF QDDQGKLNKL AFNTMRPIAQ
GGLLKYVFGE EYHAYNPDVV MQLQKAVQNG DYKEYRKYAD LVNKRPVAML RDLMGLKLDA
AKAISIDEVE SVEDILKRFD SAGMSLGALS PEAHEALAEG MNRLGGRSNS GEGGEDPARY
GTMKMSKIKQ VASGRFGVTP HYLVNAEVLQ IKVAQGAKPG EGGQLPGDKV SPLIAKLRCS
KPGISLISPP PHHDIYSIED LAQLIFDLKQ VNPEALVSVK LVAEPGVGTI AAGVAKAYAD
LITISGYDGG TGASPLASVK YAGTPFELGL TEAQQVLRAN GLRGRVRMQA DGGLKTGLDV
VKAAMMGAES FGFGTGPMVA LGCKFLRICH LNNCATGVAT QEIKLRSKYF IGLPEMVVNY
FTFIAQETRE WMAALGVRQL SDLIGHSEML ELAAGATERQ GRLKLGVLLS QGTIPESQPR
FCVEARNPSF DKGELAEEMV KDAIAGIKSQ TPQKFEYAVR NIHRSIGARL SGEIAKAHGA
DGLPNECLHI KLHGSAGQSL GVWNAKGLTI ELEGDANDYV GKGMSGGRVV VYPPKASEFE
SHAGVIVGNT CLYGATGGEL FAAGTAGERF AVRNSGATAI VEGIGDHGCE YMTGGCVIVL
GETGYNFGAG MTGGFALVYD PKERFAYRIN NELVDINLIN GESYGAVRAF LRGKLRDHAK
LTGSTRAIDI LADFDEAQDN FWLVKPKAAK LDDLLKD
//
