ID A0A0F5P6Z0_9SPHN Unreviewed; 478 AA.
AC A0A0F5P6Z0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KKC23956.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:KKC23956.1};
GN Name=gltD {ECO:0000313|EMBL:KKC23956.1};
GN ORFNames=WP12_22050 {ECO:0000313|EMBL:KKC23956.1};
OS Sphingomonas sp. SRS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=133190 {ECO:0000313|EMBL:KKC23956.1, ECO:0000313|Proteomes:UP000033680};
RN [1] {ECO:0000313|EMBL:KKC23956.1, ECO:0000313|Proteomes:UP000033680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRS2 {ECO:0000313|EMBL:KKC23956.1,
RC ECO:0000313|Proteomes:UP000033680};
RA Nielsen T.K., Sorensen S.R., Hansen L.H.;
RT "Draft genome sequence of isoproturon-mineralizing Sphingomonas sp. SRS2,
RT isolated from an agricultural field in the United Kingdom.";
RL Submitted (MAR-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:KKC23956.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LARW01000151; KKC23956.1; -; Genomic_DNA.
DR RefSeq; WP_046195807.1; NZ_LARW01000151.1.
DR AlphaFoldDB; A0A0F5P6Z0; -.
DR STRING; 133190.WP12_22050; -.
DR PATRIC; fig|133190.4.peg.1522; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000033680; 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; 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; 2.
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:KKC23956.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033680}.
FT DOMAIN 36..68
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 478 AA; 52374 MW; D438D5E9B6EE8569 CRC64;
MGKATGFLEI DRKDRGYLKP QDRLKNWNEF VVPMDAQQIR DQAARCMNCG IPFCHNGCPV
NNIIPDWNHL VYESDWKNAL EVLHSTNNFP EFTGRVCPAP CEASCTLNIE DSPVTIKSIE
CAIVDRGWEE GWILPQTPAR RTGKSVAVVG SGPAGLACAQ QLARAGHSVT LFEKNDRMGG
LLRYGIPDFK MEKHLINRRL VQMEAEGVTY RASTEVGVQV SLDSLRENFD AVVLSGGAEK
PRPLEIPGFE LQGVRFAMEF LTQQNKRNAG DDELRAAPRG SLTATGKHVV VIGGGDTGSD
CVGTSNRQGA ASVTQFEIMP KPPEKEAKAL SWPHWPLKLR TSSSHDEGCE RDWSVVTKRA
IGNNGQLTAL ECVRVEWVGG QMREVEGSEF TIKADLVLLA MGFLGPNTPG MIEQAGVDLD
ARGNVKADVT DYATSQDGIF ACGDMRRGQS LIVWAIREGR QCARAVDLHL MGATDLPR
//
