ID A0A0Q9LGC7_9MICO Unreviewed; 484 AA.
AC A0A0Q9LGC7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KRE52833.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:KRE52833.1};
GN Name=gltD {ECO:0000313|EMBL:KRE52833.1};
GN ORFNames=ASG70_15970 {ECO:0000313|EMBL:KRE52833.1};
OS Phycicoccus sp. Soil748.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736397 {ECO:0000313|EMBL:KRE52833.1, ECO:0000313|Proteomes:UP000051855};
RN [1] {ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|Proteomes:UP000051855};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE52833.1, ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|EMBL:KRE52833.1,
RC ECO:0000313|Proteomes:UP000051855};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:KRE52833.1}.
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DR EMBL; LMSC01000012; KRE52833.1; -; Genomic_DNA.
DR RefSeq; WP_056885277.1; NZ_LMSC01000012.1.
DR AlphaFoldDB; A0A0Q9LGC7; -.
DR STRING; 1736397.ASG70_15970; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000051855; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
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; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
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:KRE52833.1}.
FT DOMAIN 38..69
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 484 AA; 52471 MW; 20E1694D3CBC7390 CRC64;
MADPQGFLKT RERELPTRRP VPVRIRDWKE VYEEQELGQL QRQAGRCMDC GIPFCHSGCP
LGNLIPEWND LAWKGDWREA IERLHATNNF PEFTGRLCPA PCETACVLGI NQPAVTIKQV
EVTTIERAFD SGYVQPQAPE RLSGKTVAVV GSGPAGLAAA QQLTRAGHTV AVYERADKPG
GLLRYGIPEF KMEKSVLDRR IAQMEAEGTR FRSGVAVGED VTGRQLRDRY DAVVLAIGAT
VPRDLPVPGR ELDGVMQAMD FLPPANRAAL GEAVEGQVTA EGKDVIVIGG GDTGADCIGT
SHRQGARSVT SLEIMPQPGE ERVTGQPWPT YPMLFRVASA HEEGGERLYA VSTKEILGED
GKVSGIRVVD VQRGDHGFDE VEGTERVLPA QLVLLAMGFL GPEKPGVVEQ LEVELDERSN
VKRDKDYMSS VPGVFVAGDA GRGQSLIVWA IAEGRSAAAG VDRFLTGQTA LPRPINPNDR
PLVV
//
