ID A0A261G6H2_9BIFI Unreviewed; 1523 AA.
AC A0A261G6H2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 18-JUN-2025, entry version 26.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:OZG67037.1};
GN ORFNames=BAQU_1109 {ECO:0000313|EMBL:OZG67037.1};
OS Bifidobacterium aquikefiri.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1653207 {ECO:0000313|EMBL:OZG67037.1, ECO:0000313|Proteomes:UP000216451};
RN [1] {ECO:0000313|EMBL:OZG67037.1, ECO:0000313|Proteomes:UP000216451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 28769 {ECO:0000313|EMBL:OZG67037.1,
RC ECO:0000313|Proteomes:UP000216451};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZG67037.1}.
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DR EMBL; MWXA01000005; OZG67037.1; -; Genomic_DNA.
DR RefSeq; WP_094693487.1; NZ_CALENZ010000001.1.
DR GeneID; 98295778; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000216451; 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:0019676; P:ammonia assimilation cycle; IEA:TreeGrafter.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR FunFam; 3.20.20.70:FF:000031; Glutamate synthase 1 [NADH]; 1.
DR FunFam; 3.20.20.70:FF:000053; Glutamate synthase large subunit; 1.
DR FunFam; 2.160.20.60:FF:000001; Glutamate synthase, large subunit; 1.
DR FunFam; 3.60.20.10:FF:000001; Glutamate synthase, large subunit; 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; IPR050711; ET-N_metabolism_enzyme.
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 NCBIfam; NF008730; PRK11750.1; 1.
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 FAD {ECO:0000256|ARBA:ARBA00022827};
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:UP000216451}.
FT DOMAIN 27..414
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 906..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1523 AA; 166830 MW; 70561A3814AD9379 CRC64;
MTFKAPLDLT VHNAQGLYDP ANEHDACGVG MVTTLNGLPE RSIVDHAIEV LVNLDHRGAV
GAEKNTGDGA GMLITMPDEF MRATIEAELP EQGSYAAGIV FLDRDIALGA QQEQAIASIV
EEEGLSVLAW RDVPTNPNGL GLQALSTMPS FKTLVIADPT GGLKGMDLER RAFRVRKRVE
HAVGVYFASL STKTITYKGM LTTMQLQPFF PDLSNPLMKA RIAIVHSRFS TNTFPSWPLA
QPFRLLAHNG EINTIQGNRN WVSAREGRLS SELLGDISQL LPINTPGYSD SGTFDETLEL
LYLAGRSLPH AVSMMLPPAW EKDDTLDPDV RAFYEYNNTL IEPWDGPANI IFTDGDLVGA
QLDRNGLRPG RWQLMDDGHL VLASETGVLD KIPQSHIARK GRLEPGKMFL VDVNEGRIVP
DGEIRKDLAS QHPYRSWVEG NSVEMSELPA REHVSHSGMS VQRRQRAFGY TEEDLKMLLA
PMADGGKEPL GAMGNDTPMA VLSSRSRMLF DYFTQKFAQV TNPPLDWERE EIVTCLESAI
GPEPNLLEDT ELHAKKILIP NPVVDSDEMA QLKRLDKAQI LNNYYKPFVV KGLYQVAGGG
KALKARLDEI FKQIDDAIDV GKNFIVLSDR DSNHTWGPIP SLLMTSAVQH HLLRRHTRTQ
VSLAVEAGDV REVHHVALLI AYGAACVNPY LALESVENLS ERGYLKVTGE QAAKNLTKAL
STGVLKIMSK MGVSTIMSYR GSQLFEAIGL SQEIVDEYFT GTTSRVGGTG LDEIAEEVAI
RHRVAYPTQW TARPHRNLRS GGDYKWRRTG EEHLNDPESI FLLQQSTQRA DYTMFKQYSH
HINDTSNRLM TLRGLMKFNH KRKPIDISEV EPASEIVKRF STGAMSYGSI SQEAHETLAK
AMNKLGARSN SGEGGESQDR IEDPARTSRI KQIASARFGV TSDYLVSATD LQIKLAQGAK
PGEGGHLPGA KVPPWIAEVR RATPGVELIS PPPHHDIYSI EDLKQLINDA KMANPKARIH
VKLVSEFGVG TIAAGVAKCY ADVVLISGYD GGTGAAPLNA IKHAGTPWEI GLSETQQTLI
LNGLRSRIVV QCDGELKTGR DVVIAALLGA EEFGFATAAL IVEGCVMMRA CQLNTCPQGI
ATQDPELRAR FRGKPEHVIN FFMFIAEEVR ELLAQLGFHT LEEAVGHVEM LDQNEAISRW
KSGGIDLSNV LMQAGPTPGT ILHHTINQNH ELEKALDNRL IKLAEPALDR KEPVLIDVPI
RNVNRTVGTM LGYEITKRYK AQGLPDDTID ITLHGSGGQS IGAFIPRGET LRIYGEVNDY
AGKGLSGGRI IVRPAEDIHF DPHENVICGN VTGFGATSGQ MLIAGKAGER FAVRNGGASF
VVEGVGDHGC EYMTGGTVAI LGPTGRNFGA GFSGGNAYVL DLDMDKVNPS ARVNGSLKFL
AVEAEYAEEL HALVKHHAEE TGSETAKNLL KDWKTSIARF THVVPTQYLA MKTAMDQAHK
DNVDFNQPGA WESLYERVVE GVH
//
