ID A0A086ZRT7_9BIFI Unreviewed; 1507 AA.
AC A0A086ZRT7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glutamate synthase, alpha subunit {ECO:0000313|EMBL:KFI49237.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:KFI49237.1};
GN ORFNames=BBOU_0100 {ECO:0000313|EMBL:KFI49237.1};
OS Bifidobacterium boum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=78343 {ECO:0000313|EMBL:KFI49237.1, ECO:0000313|Proteomes:UP000029093};
RN [1] {ECO:0000313|EMBL:KFI49237.1, ECO:0000313|Proteomes:UP000029093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 10736 {ECO:0000313|EMBL:KFI49237.1,
RC ECO:0000313|Proteomes:UP000029093};
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:KFI49237.1}.
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DR EMBL; JGYQ01000002; KFI49237.1; -; Genomic_DNA.
DR Proteomes; UP000029093; 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:KFI49237.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029093}.
FT DOMAIN 11..398
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1507 AA; 165435 MW; 7DD41400EF197C09 CRC64;
MYDPSQEHDA CGVGMVTTLN KRPERKIVDD AIEVLVNLNH RGAVGAEENT GDGAGILMAM
PDEFMRATTG VELPEAGHYA AGIAFLDRDI ATSGQQEQAI AKIVNEEGLE VLAWRVVPTN
PDGLGLQALA SMPSFKTLVV ADPENKLSGI DLDRKTFRIR KRVEHEVGIY FASLSARTIT
YKGMLTTMQL TGFFPDLLDE RMKTTIAIVH SRFSTNTFPS WPLAQPFRLI AHNGEINTIQ
GNRNWLSARE GRLSSELLGE FKPLLPIATP GYSDSGTFDE CLELLHLAGR SLPHALLMML
PPAWENDDTL DPEVKAFYEY NNTLIEPWDG PADIVFTDGT LVGAQLDRNG FRPGRWQLTD
NGYLVLASEA GVLPEISQDH IVAKGRLEPG KMFLVDTKAG RIVPDDEIKH DLASQHPYRK
WIEGNSVEMS QLPVREHVSH FGQSVQRRQR AFGYTEEDLK LLLAPMANTG KEPLGSMGSD
TPPAVLSKRS RMLFDYFTQK FAQVTNPPLD WERERIVTSL ESAIGPEANL LQDTELHAKK
ILIPLPVIDS DQMAQLKRLD KAKILGGFYK PFVVRGLYQV AGGGKALKER LEEIFQEVDD
AIADGKNFIV LSDRESDHTW GPIPSLLLTS AVQHHLLRRH TRTQVSLAVE AGDVREIHHV
ALLIAYGAAC VNPYLAFESV EELARTGYLK VDAPTAVKNL TNALSTGVLK IMSKMGVSTI
MSYRGAQLFE AVGLNQEVID EYFTGTTSRV GGAGLDEIAE EVAIRHRVAY PNQWTSRPHR
NLRTGGDYKW RRTGEDHLND PEAIFLLQQA TQRGDYNLFK KYSAHINDTS NRLMTLRGLM
KFKQTRKPID ISEVEPASEI VKRFSTGAMS YGSISQEAHE TLAIAMNTIG ARSNSGEGGE
SDDRINDPLR YSRIKQIASA RFGVTSDYLV HATDLQIKLA QGAKPGEGGH LPGAKVPPWI
AKVRHATPGV ELISPPPHHD IYSIEDLKQL INDAKMANPK ARVHVKLVSE FGVGTIAAGV
AKCHADVVLI SGSDGGTGAA PLNAIKHAGT PWEIGLAETQ QTLILNGLRS RIVVQCDGEL
KTGRDVVIAA LLGAEEFGFA TAALITEGCV MMRACQKNTC PQGIATQDPE LRARFRGKPE
YVINFFMYIA QEVRELLAQL GFRTLEEAVG HVECLDQNDA VARWKADGID LSNVLMQPGP
IPGTILHQTI EQNHELEKAL DNKLIELAQP ALEHKEPVRI EMPIRNVNRT LGTMVGYEIT
RRYGAPGLPD DTIDMTFHGS GGQSIGAFIP RGETIRVYGE VNDYAGKGLS GGRMVVRPEQ
DITFDPHTNV IAGNVTGFGA TSGEMFVAGR AGERFAVRNG GATFVVEGVG DHGCEYMTGG
VVVILGAMGR NFGAGFSGGD TYVLDLDMRQ VNPDACKSGA LLFEPLEGAD EQLVHDLIKR
HVEETGSVFA QGLLDDWEHT RTRITHVTPK HYVAMTKAME QAKENNVDFN APGAWEHVYE
QVMEGAH
//
