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Database: UniProt
Entry: A0A0A7I7T8_9BIFI
LinkDB: A0A0A7I7T8_9BIFI
Original site: A0A0A7I7T8_9BIFI 
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
//
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