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Database: UniProt
Entry: A0A087CUZ3_9BIFI
LinkDB: A0A087CUZ3_9BIFI
Original site: A0A087CUZ3_9BIFI 
ID   A0A087CUZ3_9BIFI        Unreviewed;       512 AA.
AC   A0A087CUZ3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Glutamate synthase subunit beta {ECO:0000313|EMBL:KFI87093.1};
DE            EC=1.4.1.13 {ECO:0000313|EMBL:KFI87093.1};
GN   ORFNames=BREU_0112 {ECO:0000313|EMBL:KFI87093.1};
OS   Bifidobacterium reuteri DSM 23975.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437610 {ECO:0000313|EMBL:KFI87093.1, ECO:0000313|Proteomes:UP000028984};
RN   [1] {ECO:0000313|EMBL:KFI87093.1, ECO:0000313|Proteomes:UP000028984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23975 {ECO:0000313|EMBL:KFI87093.1,
RC   ECO:0000313|Proteomes:UP000028984};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:KFI87093.1}.
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DR   EMBL; JGZK01000003; KFI87093.1; -; Genomic_DNA.
DR   RefSeq; WP_044088310.1; NZ_JGZK01000003.1.
DR   AlphaFoldDB; A0A087CUZ3; -.
DR   STRING; 1437610.BREU_0112; -.
DR   eggNOG; COG0493; Bacteria.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000028984; Unassembled WGS sequence.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR006005; Glut_synth_ssu1.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
DR   PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 2.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KFI87093.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028984}.
FT   DOMAIN          41..129
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          147..478
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   512 AA;  56334 MW;  033A47001E92566C CRC64;
     MGDPRGFLKV RTRRELAERP IEERIKDWFD VHAESGLQPW TREQAARCMD CGTPFCMTGC
     PLGNIIPEFN DLVRQAKWED AYNRLSQTNN FPEVTGRICP ALCEQACVLG IHQPPTMIKN
     DECTIIDQAW DLDYVKPLPP QRLTDQTVAI VGSGPAGLAA AQQLTRAGHT VVVYEKDDAI
     GGLMRYGIPN FKLEKGLLDR RVEQMEAEGT RFRTNVEIGK DISWDELRDR YDAVVVAIGS
     RVPRDMKIPG RELDGIHFAL DFLPDATRRV FGVKPVNDIT AKDKHVIVIG GGDTGSDCLG
     TSIRQGAKDV TVLQIMPKEP ESRPANQPWP TFARTYQKTT SMAEGGTYLY STDSVNFIGS
     EEEQAKVKIE NSTTAEGFVA DEHGHVTGLK VVSVAPGENG PFTRQPGTER VLPADLVLIS
     VGFLHPDTTT LLDQLPVELD KRGNIARNDK FATSQDGVFV CGDAGRGQSL VVWAIAEGRS
     CAAAVDEYLS SEKTSELPAP IKASDRPMML PR
//
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