ID A0A0A7I7T8_9BIFI Unreviewed; 511 AA.
AC A0A0A7I7T8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
GN Name=gltD {ECO:0000313|EMBL:AIZ16332.1};
GN ORFNames=AH67_04805 {ECO:0000313|EMBL:AIZ16332.1};
OS Bifidobacterium pseudolongum PV8-2.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1447715 {ECO:0000313|EMBL:AIZ16332.1, ECO:0000313|Proteomes:UP000030636};
RN [1] {ECO:0000313|EMBL:AIZ16332.1, ECO:0000313|Proteomes:UP000030636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV8-2 {ECO:0000313|EMBL:AIZ16332.1,
RC ECO:0000313|Proteomes:UP000030636};
RX PubMed=25614573;
RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Stevens M.J.,
RA Jans C.;
RT "Bifidobacterium pseudolongum Strain PV8-2, Isolated from a Stool Sample of
RT an Anemic Kenyan Infant.";
RL Genome Announc. 3:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine
CC + NADPH; Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58359; EC=1.4.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001895};
CC -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+)
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00037898}.
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DR EMBL; CP007457; AIZ16332.1; -; Genomic_DNA.
DR RefSeq; WP_026647810.1; NZ_CP007457.1.
DR AlphaFoldDB; A0A0A7I7T8; -.
DR STRING; 1447715.AH67_04805; -.
DR GeneID; 61075848; -.
DR KEGG; bpsp:AH67_04805; -.
DR HOGENOM; CLU_000422_3_1_11; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000030636; Chromosome.
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; 2.
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:AIZ16332.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030636}.
FT DOMAIN 40..120
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 511 AA; 55780 MW; 2DA6CFB662193538 CRC64;
MGDPRGFLKV RTRHELAERP VEERIKDWLD VHAESGLQSW TQEQAARCMD CGTPFCMSGC
PLGNLIPEWN DLVRQGQWLE AYNRLSMTNN FPEVTGRICP ALCESSCVLG IHQPPTMIKL
DEVTAIDQAW ELDYVKPLPP ERLSGQTVAV VGSGPAGLAC AQQLTRTGHT VVVFERDDEV
GGLMRYGIPN FKLDKGLIDR RVEQMKAEGT RFRTNTEVGK DISWDALRAS YDAVVVAIGS
TVPRDMNIPG RQLDGIHFAM EFLPDATRRF YGKQPVHDIT AEGKHVVIIG GGDTGSDCLG
TSIRQGAKDV TVLQIMPQEP TSRPDNQPWP TFARLYQKTS SMEEGGEYIY NTDSVSFEGT
AEQEARISVE HGTQAEGFVA DAQGHVTGLK VVSVAPGDDG PFTRQPGTER VLPADLVLIS
VGFLHPDTTT LVDQLPVELD NRGNVARDDA YATSQDGVFA CGDAGRGQSL VVWAIAEGRS
CAAAVDQYLM GSTELPSPIV ASERPMALPR R
//