ID D2QA81_BIFDB Unreviewed; 515 AA.
AC D2QA81;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Glutamate synthase [NADPH] small subunit {ECO:0000313|EMBL:ADB09717.1};
DE EC=1.3.1.2 {ECO:0000313|EMBL:ADB09717.1};
GN OrderedLocusNames=BDP_1079 {ECO:0000313|EMBL:ADB09717.1};
OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB09717.1, ECO:0000313|Proteomes:UP000008693};
RN [1] {ECO:0000313|EMBL:ADB09717.1, ECO:0000313|Proteomes:UP000008693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC {ECO:0000313|Proteomes:UP000008693};
RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT adaptation to the human oral cavity.";
RL PLoS Genet. 5:E1000785-E1000785(2009).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; CP001750; ADB09717.1; -; Genomic_DNA.
DR RefSeq; WP_003840258.1; NC_013714.1.
DR AlphaFoldDB; D2QA81; -.
DR STRING; 401473.BDP_1079; -.
DR GeneID; 69536739; -.
DR KEGG; bde:BDP_1079; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_1_11; -.
DR Proteomes; UP000008693; Chromosome.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:RHEA.
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; 3.
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:ADB09717.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008693}.
FT DOMAIN 40..128
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 147..483
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 515 AA; 56543 MW; E7113FECAD893E00 CRC64;
MGDPRGFLKV RTRRELAERP IEERIKDWFD VHAESGLQPW TTEQAARCMD CGTPFCMSGC
PLGNIIPEFN DLVRQEKWED AYNRLSETNN FPEVTGRICP ALCEAACVLG IHQPATMIRN
DECTIIDQAW DLDYVRPLPP QRLTDQTVAV VGSGPSGLAC AQQLTRAGHT VVVYERDDAI
GGLMRYGIPN FKLDKRLIDR RVEQMEAEGT VFRTGVEIGK DISWDDLRSR YDAVVVAIGS
TVPRDMKIPG RELKGIHFAM EFLPDATRRV YGVKPVNDIT AEGKHVVIIG GGDTGSDCLG
TSIRQGAKDV TVLQIMPQEP TERPGNQPWP TFARLYQKTT SMDEGFETQR AEYVYSTDSV
NFVGTEEEQA KVKVEDATAT EGFVADENGH VTGLKVVNVA PGENGPFTRQ PGTERVIPAD
LVLISVGFLH PDTTTLVDQL PVDLDGRGNV ARNDKFATSQ DGVFACGDAG RGQSLVVWAI
SEGRSCAAAV DEYLTGSTEL PAPIVASKRP MMLPR
//
