ID B1T5U4_9BURK Unreviewed; 488 AA.
AC B1T5U4;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Glutamate synthase, NADH/NADPH, small subunit {ECO:0000313|EMBL:EDT41052.1};
GN ORFNames=BamMEX5DRAFT_3160 {ECO:0000313|EMBL:EDT41052.1};
OS Burkholderia ambifaria MEX-5.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396597 {ECO:0000313|EMBL:EDT41052.1, ECO:0000313|Proteomes:UP000004814};
RN [1] {ECO:0000313|EMBL:EDT41052.1, ECO:0000313|Proteomes:UP000004814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEX-5 {ECO:0000313|EMBL:EDT41052.1,
RC ECO:0000313|Proteomes:UP000004814};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Tiedje J., Richardson P.;
RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria MEX-
RT 5.";
RL Submitted (MAR-2008) 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:EDT41052.1}.
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DR EMBL; ABLK01000093; EDT41052.1; -; Genomic_DNA.
DR RefSeq; WP_006759044.1; NZ_ABLK01000093.1.
DR AlphaFoldDB; B1T5U4; -.
DR PATRIC; fig|396597.7.peg.4837; -.
DR Proteomes; UP000004814; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; 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; 1.
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; 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}.
FT DOMAIN 37..68
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 488 AA; 53612 MW; 9DCB6DF7120981EA CRC64;
MGKATGFLEF ERRHEAYEAP LTRVKHYKEF VAALTDADAK VQGARCMDCG IPFCNNGCPV
NNIIPDFNDL VYRQDWQQAI EVLHSTNNFP EFTGRICPAP CEAACTLGIN DDPVGIKSIE
HAIIDKAWAE GWVKPLPPEH KTGKTVAVVG SGPAGLAVAQ QLARAGHDVT VFEKNDRIGG
LLRYGIPDFK LEKWLIDRRM RQMEAEGVTF RTSVFIGKDP LPESIGSLAK ETISPEQLKE
EFDAVVIAGG SETPRDLPVP GRELAGVHFA MDFLPQQNRV NAGDKLVDQL VAKGKHVIVI
GGGDTGSDCV GTSNRHGAKQ VTQFELLPQP PEEENKPLVW PYWPIKLRTS SSHEEGCERD
WAVATKRLEG KNGKVEKLIA VRVEWKDGKM QEVPGSEFEL KADLVLLAMG FTQPAATVLE
AFGVAKDARG NARAATEGDR SYYTSVDKVF AAGDMRRGQS LVVWAIREGR QCARSVDAYL
MGHSNLPR
//
