ID   GLTD_AZOBR              Reviewed;         482 AA.
AC   Q05756; Q9EXL4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 77.
DE   RecName: Full=Glutamate synthase [NADPH] small chain;
DE            EC=1.4.1.13;
DE   AltName: Full=Glutamate synthase subunit beta;
DE            Short=GLTS beta chain;
DE   AltName: Full=NADPH-GOGAT;
GN   Name=gltD;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-24;
RP   183-204 AND 328-344.
RC   STRAIN=ATCC 29145 / Sp7 / DSM 1690 / IMET 11303;
RX   MEDLINE=93155143; PubMed=8428988;
RA   Pelanda R., Vanoni M.A., Perego M., Piubelli L., Galizzi A., Curti B.,
RA   Zanetti G.;
RT   "Glutamate synthase genes of the diazotroph Azospirillum brasilense.
RT   Cloning, sequencing, and analysis of functional domains.";
RL   J. Biol. Chem. 268:3099-3106(1993).
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Vanoni M.A., Verzotti E., Morandi P., Curti B.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=90335272; PubMed=2198943; DOI=10.1016/0167-4838(90)90273-I;
RA   Vanoni M.A., Negri A., Zanetti G., Ronchi S., Curti B.;
RT   "Structural studies on the subunits of glutamate synthase from
RT   Azospirillum brasilense.";
RL   Biochim. Biophys. Acta 1039:374-377(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-8.
RC   STRAIN=Sp6;
RX   PubMed=8001567; DOI=10.1111/j.1432-1033.1994.tb20075.x;
RA   Vanoni M.A., Mazzoni A., Fumagalli P., Negri A., Zanetti G., Curti B.;
RT   "Interdomain loops and conformational changes of glutamate synthase as
RT   detected by limited proteolysis.";
RL   Eur. J. Biochem. 226:505-515(1994).
CC   -!- CATALYTIC ACTIVITY: 2 L-glutamate + NADP(+) = L-glutamine + 2-
CC       oxoglutarate + NADPH.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC       pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADPH
CC       route): step 1/1.
CC   -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC   -!- SUBUNIT: Aggregate of 4 catalytic active heterodimers, consisting
CC       of a large and a small subunit.
CC   -!- MISCELLANEOUS: Glutamine binds to the large subunit and transfers
CC       the amido group to 2-oxo-glutamate that apparently binds to the
CC       small subunit.
CC   -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain.
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DR   EMBL; AF192408; AAG38999.1; -; Genomic_DNA.
DR   PIR; A46602; A46602.
DR   PDB; 2VDC; EM; 9.50 A; G/H/I/J/K/L=27-482.
DR   PDBsum; 2VDC; -.
DR   BioCyc; MetaCyc:MON-13080; -.
DR   BRENDA; 1.4.1.13; 1315.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000759; Adrndx_reductase.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR012285; Fum_reductase_C.
DR   InterPro; IPR006006; Glut_synth_sub2.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   Gene3D; G3DSA:1.10.1060.10; Fum_reductase_C; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR01318; gltD_gamma_fam; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Amino-acid biosynthesis;
KW   Direct protein sequencing; Glutamate biosynthesis; Iron; Iron-sulfur;
KW   Metal-binding; NADP; Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    482       Glutamate synthase [NADPH] small chain.
FT                                /FTId=PRO_0000170799.
FT   DOMAIN       39     72       4Fe-4S ferredoxin-type.
FT   METAL        95     95       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL        99     99       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       105    105       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       109    109       Iron-sulfur (4Fe-4S) (Potential).
SQ   SEQUENCE   482 AA;  52358 MW;  8224C1B4EAAFCB25 CRC64;
     MANQRMLGFV HTAQRMPDKR PAAERRQDFA EIYARFSDER ANEQANRCSQ CGVPFCQVHC
     PVSNNIPDWL KLTSEGRLEE AYEVSQATNN FPEICGRICP QDRLCEGNCV IEQSTHGAVT
     IGSVEKYIND TAWDQGWVKP RTPSRELGLS VGVIGAGPAG LAAAEELRAK GYEVHVYDRY
     DRMGGLLVYG IPGFKLEKSV VERRVKLLAD AGVIYHPNFE VGRDASLPEL RRKHVAVLVA
     TGVYKARDIK APGSGLGNIV AALDYLTTSN KVSLGDTVEA YENGSLNAAG KHVVVLGGGD
     TAMDCVRTAI RQGATSVKCL YRRDRKNMPG SQREVAHAEE EGVEFIWQAA PEGFTGDTVV
     TGVRAVRIHL GVADATGRQT PQVIEGSEFT VQADLVIKAL GFEPEDLPNA FDEPELKVTR
     WGTLLVDHRT KMTNMDGVFA AGDIVRGASL VVWAIRDGRD AAEGIHAYAK AKAEAPVAVA
     AE
//