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
//