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Database: UniProt
Entry: A0A0D0UPW7_9ACTN
LinkDB: A0A0D0UPW7_9ACTN
Original site: A0A0D0UPW7_9ACTN 
ID   A0A0D0UPW7_9ACTN        Unreviewed;       501 AA.
AC   A0A0D0UPW7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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:KIR60917.1};
GN   ORFNames=TK50_24175 {ECO:0000313|EMBL:KIR60917.1};
OS   Micromonospora haikouensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=686309 {ECO:0000313|EMBL:KIR60917.1, ECO:0000313|Proteomes:UP000032254};
RN   [1] {ECO:0000313|EMBL:KIR60917.1, ECO:0000313|Proteomes:UP000032254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR60917.1,
RC   ECO:0000313|Proteomes:UP000032254};
RA   Long Z., Huang Y., Jiang Y.;
RT   "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1
RT   genome.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KIR60917.1}.
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DR   EMBL; JXSX01000003; KIR60917.1; -; Genomic_DNA.
DR   RefSeq; WP_043967390.1; NZ_JXSX01000003.1.
DR   AlphaFoldDB; A0A0D0UPW7; -.
DR   PATRIC; fig|47853.6.peg.5066; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000032254; 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; 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:KIR60917.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032254}.
FT   DOMAIN          24..129
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          145..470
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   501 AA;  52930 MW;  3CA7239D380F235C CRC64;
     MPDPNGFLRY DRRLPARRPV PVRITDWREV YPPAGEALIR EQATRCMDCG IPFCHDGCPL
     GNRIPDWNDL VRTGGWDAAV ESLHATNNFP EFTGRLCPAP CEAACVLGIG GGQPVTIKQV
     EVEIADAAAR GGLAPRPAPA PTGRSVAVVG SGPAGLAAAQ QLARAGHAVT VYERDDAIGG
     LLRYGIPDFK LEKQHIDLRL AQLEAEGVRF RTGVHVGVDV TAEQLREAHD AVLLACGALQ
     GRDTPETPGR ALRGVHQAMA HLVAANRVVA AAGEGRPALA VLPDGTPIDA AGKHVVIIGG
     GDTAADCLGV AHRQGAAGVH QLDLYPEPPH ARDAARDPWP TWPWILRSYP AHEEGGDRVF
     AAAVQEFVDD GTGQVRAVRI AEVTVEKRDG RRIVTAVPGS ERELPADLVL LAIGFEGTEE
     QPLLAQFGVA RNARGAIDAR PDWQTDADGV FVAGDMHRGA SLIVWAIAEG RAAAAAIHSY
     LGGVGELPAP VDPARQPLAA R
//
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