ID A0A087B4L3_9BIFI Unreviewed; 1506 AA.
AC A0A087B4L3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KFI65963.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:KFI65963.1};
GN ORFNames=BCUN_0462 {ECO:0000313|EMBL:KFI65963.1};
OS Bifidobacterium cuniculi.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1688 {ECO:0000313|EMBL:KFI65963.1, ECO:0000313|Proteomes:UP000029067};
RN [1] {ECO:0000313|EMBL:KFI65963.1, ECO:0000313|Proteomes:UP000029067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 10738 {ECO:0000313|EMBL:KFI65963.1,
RC ECO:0000313|Proteomes:UP000029067};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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}.
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:KFI65963.1}.
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DR EMBL; JGYV01000001; KFI65963.1; -; Genomic_DNA.
DR RefSeq; WP_051920653.1; NZ_JGYV01000001.1.
DR STRING; 1688.BCUN_0462; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000029067; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:KFI65963.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029067}.
FT DOMAIN 11..398
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1506 AA; 164079 MW; 31489BB4364DFD8C CRC64;
MYDPASEHDA CGVGMVTTLN GKPERKIVDD AIEVLVNLNH RGAVGAEENT GDGAGILMAM
PDEFMRATVD ADLPAAGHYA AGIAFLDRDI AVCGQQEQAI ARIAAEEGLA VLAWRQVPTD
PNGLGLQALA SMPAFKTLVL ADPDGRLGGI ELDRRVYHVR KRAEHEVGIY FASLSSRTIT
YKGMLTTMQL KPFFPDLSDE RMKTTIAIVH SRFSTNTFPS WPLAQPFRML AHNGEINTIQ
GNRNWFTARQ GRLKSELLGD MADLLPILTP GYSDSGTFDE VLELLNLAGR SLPHAVLMMV
PPAWEKDPGL DPDVRAFYEY NNSLIEPWDG PADIVFTDGT LVGAVLDRNG FRPGRWQVDD
AGYVVLASEA GVLPQVPDGC VVAKGRLEPG RMFLIDTAAG RIIPDAEIKH DLATQHPYRE
WVEDNSVDMA DLPRREHISY SDQSVHRRQR AFGYTQEELK LVLTPMANTG KEPLGSMGND
TPLSVLSGRS RMLFDYFTQK FAQVTNPPLD WEREKIVTSI ESAIGPEPNL LEDCATHAKK
IVIAQPVIDN DEMAKLKRIN RARQLDGYYQ PYVVKGLYEV TGGGDALARR LEEIFAEVDE
AIAQGCNFLV LSDRDSDHMM APIPSLLLTS AVQHHLLRRQ TRTQISMVVE AGDVREIHHV
ALLIAYGAAA VNPYLAFESV EELARTGFLA VDGERGIANL RQALSTGVLK IMSKMGVSTI
MSYRGAQLFE AVGLNSDVID AYFTGTVSRV DGCGLDELAE EVAIRHREAY PNQWSARPHR
ELPTGGDYKW RRTGEEHLND PEAIFLLQQS TQRGDYAMFK QYSAHVNDTS NRLMTLRGLM
KFNHVRPAVD ISEVEPASEI VKRFSTGAMS YGSISKEAHE TLAIAMNSIG ARSNSGEGGE
STERLNDPLL CSKIKQIASA RFGVTSDYLV HATDLQIKLA QGAKPGEGGH LPGAKVPPWI
AKVRHATPGT ELISPPPHHD IYSIEDLKQL INDAKMSNPK ARIHVKLVSE FGVGTIAAGV
AKCHADVVLI SGYDGGTGAA PLNAIRHAGT PWEIGLSETQ QTLILNGLRS RITVQCDGEL
KTGRDVIVAA LLGAEEFGFA TTALMVEGCV MMRACQKNTC PQGIATQDPE LRARYTGKPE
HVINFMMFIA EEVRELLAEL GFRTLEEAVG HVECLDQDEA IKRWKSAGVD LANVLMQPGP
VPGTVLHQTI EQNHELDKAL DNELIAQAAP ALERGEHVDI AMDIRNVNRT LGTMLGYEIT
RRTGEAGLPD DTVELTLHGT GGQSIGAFIP RGETLHIVGE VNDYAGKGLS GGSIDIRAPH
DVTYDPHENV IAGNVLGFGA TSGTMFVAGR AGERFGVRNG GATFVVEGVG DHGCEYMTGG
TVVILGPTGR NLGAGFSGGH VYALDLDMDK VNPQAAAGSL LFEPLDDESA DTVRTLVQEH
VARTGSAFAQ GLLDDWEQAR GRFTHMVPRM FVAMTEAMAQ AKAEHIDFNE PGVWEHTYEQ
VMEGAR
//
