ID Q13TM2_PARXL Unreviewed; 489 AA.
AC Q13TM2;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Glutamate synthase (NADH) small subunit {ECO:0000313|EMBL:ABE32567.1};
DE EC=1.4.1.14 {ECO:0000313|EMBL:ABE32567.1};
GN ORFNames=Bxe_A0366 {ECO:0000313|EMBL:ABE32567.1};
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE32567.1, ECO:0000313|Proteomes:UP000001817};
RN [1] {ECO:0000313|EMBL:ABE32567.1, ECO:0000313|Proteomes:UP000001817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400 {ECO:0000313|EMBL:ABE32567.1,
RC ECO:0000313|Proteomes:UP000001817};
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; CP000270; ABE32567.1; -; Genomic_DNA.
DR RefSeq; WP_011490025.1; NZ_CP008760.1.
DR AlphaFoldDB; Q13TM2; -.
DR STRING; 266265.Bxe_A0366; -.
DR KEGG; bxb:DR64_2536; -.
DR KEGG; bxe:Bxe_A0366; -.
DR PATRIC; fig|266265.5.peg.4256; -.
DR eggNOG; COG0493; Bacteria.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000001817; Chromosome 1.
DR GO; GO:0016040; F:glutamate synthase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:RHEA.
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:ABE32567.1}.
FT DOMAIN 37..68
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 489 AA; 53751 MW; 9309DF4B7B6BAFBA CRC64;
MGKATGFLEF ERRHEAYEAP LTRVKHYKEF VAALSDEEAK IQGARCMDCG IPFCNNGCPV
NNIIPDFNDL VFHQDWKNAI EVLHSTNNFP EFTGRICPAP CEAACTLGIN NDPVGIKSIE
HAIIDKAWTE GWVAPLPPKH KTGKKVAVVG SGPAGLAVAQ QLARAGHDVT VFEKNDRIGG
LLRYGIPDFK LEKWLIDRRM RQMEAEGVTF RANVFIGKAD SLPAHIGNTA KETITPDQLK
EEFDAVVIAG GSETPRDLPV PGRELEGIHY AMEFLPQQNK VNAGDKVANQ LLAKGKHVVV
IGGGDTGSDC VGTSNRHGAK SVTQFELLPQ PPEEENKPLV WPYWPIKLRT SSSHDEGCSR
DWAVATKRLE GKNGKVEKLI AARVEWKDGK MQEVPGSEFE MKADLVLLAM GFTQPVSPVL
EAFGVDKDAR GNVRSSTEGD KAYYTSVDKV FTAGDMRRGQ SLVVWAIREG RQCARSVDAF
LMGHSELPR
//
