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Database: UniProt
Entry: I3U877_ADVKW
LinkDB: I3U877_ADVKW
Original site: I3U877_ADVKW 
ID   I3U877_ADVKW            Unreviewed;       488 AA.
AC   I3U877;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Glutamate synthase subunit beta {ECO:0000313|EMBL:AFK61215.1};
DE            EC=1.4.1.13 {ECO:0000313|EMBL:AFK61215.1};
GN   Name=gltD {ECO:0000313|EMBL:AFK61215.1};
GN   OrderedLocusNames=TKWG_03095 {ECO:0000313|EMBL:AFK61215.1};
OS   Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS   (Tetrathiobacter kashmirensis).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae.
OX   NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK61215.1, ECO:0000313|Proteomes:UP000005267};
RN   [1] {ECO:0000313|EMBL:AFK61215.1, ECO:0000313|Proteomes:UP000005267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17095 / LMG 22695 / WT001
RC   {ECO:0000313|Proteomes:UP000005267};
RX   PubMed=21914874; DOI=10.1128/JB.05781-11;
RA   Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT   "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT   Tetrathiobacter kashmirensis.";
RL   J. Bacteriol. 193:5553-5554(2011).
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR   EMBL; CP003555; AFK61215.1; -; Genomic_DNA.
DR   RefSeq; WP_014749306.1; NC_017964.1.
DR   AlphaFoldDB; I3U877; -.
DR   STRING; 1036672.TKWG_03095; -.
DR   KEGG; aka:TKWG_03095; -.
DR   HOGENOM; CLU_000422_3_1_4; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000005267; 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; 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; 2.
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:AFK61215.1}.
FT   DOMAIN          37..68
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   488 AA;  53463 MW;  BFF8844BA2335BC0 CRC64;
     MGKITGFIEF ERVAESYEAP GTRLKHYKEF VLALDDKQAQ VQGARCMDCG IPFCNTGCPV
     NNIIPDWNDL VYRQQWKQAL EVLHSTNNFP EFTGRICPAP CEEACTLNIN NDPVGIKSIE
     HAIIDKGWSE GWVVPQPPLK KTGKKVAVVG SGPAGLAAAQ QLGRAGHSVT VFEKSNRIGG
     LMRYGIPDFK LDKSLIERRV SQMEAEGVEF QASTYVGAAG DATEDGLNVI TTAELDQQFD
     AVIMAGGAEM PRDLPVPGRE LSGVHFAMDF LRQQNKRNAG DRIANQISAA GKHVIVIGGG
     DTGSDCVGTS NRQGAASVTQ IELMPRPPEH ENKALTWPYW PAKLRTSSSH LEGCERDWAI
     TTKCFKGDKG KLKKLVCTRV EWVKDEATGQ MKMQEIEGSE FELKADLVFL AMGFVSPVAA
     VLDAFGVDKD QRGNVKANVD NYRSSRDKVF AAGDMRRGQS LVVWAIREGR QCARAVDEFL
     MGTSLLPR
//
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