ID   GLTD_AZOBR     STANDARD;      PRT;   481 AA.
AC   Q05756; Q9EXL4;
DT   01-FEB-1995 (Rel. 31, Created)
DT   25-OCT-2004 (Rel. 45, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Glutamate synthase [NADPH] small chain (EC 1.4.1.13) (Glutamate
DE   synthase beta subunit) (NADPH-GOGAT) (GLTS beta chain).
GN   Name=gltD;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 1-23; 182-203 AND
RP   327-343.
RC   STRAIN=Sp7 / ATCC 29145;
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 1-7.
RC   STRAIN=Sp6;
RX   PubMed=8001567;
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: Nitrogen metabolism, glutamate biosynthesis. The
CC       catalyzed reaction brings together the nitrogen and carbon
CC       metabolism.
CC   -!- SUBUNIT: Aggregate of 4 catalytical active heterodimers,
CC       consisting 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 type ferredoxin domain.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AF192408; AAG38999.1; -.
DR   PIR; A46602; A46602.
DR   InterPro; IPR000759; Adrndx_reductase.
DR   InterPro; IPR001327; FAD_pyr_redox.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR000205; NAD_BS.
DR   InterPro; IPR000103; Pyridine_redox_2.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   TIGRFAMs; TIGR01318; gltD_gamma_fam; 1.
KW   4Fe-4S; Direct protein sequencing; Glutamate biosynthesis;
KW   Iron-sulfur; NADP; Oxidoreductase.
FT   INIT_MET      0      0
FT   METAL        94     94       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL        98     98       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       104    104       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       108    108       Iron-sulfur (4Fe-4S) (Potential).
SQ   SEQUENCE   481 AA;  52227 MW;  0A2ADC15CF426A00 CRC64;
     ANQRMLGFVH TAQRMPDKRP AAERRQDFAE IYARFSDERA NEQANRCSQC GVPFCQVHCP
     VSNNIPDWLK LTSEGRLEEA YEVSQATNNF PEICGRICPQ DRLCEGNCVI EQSTHGAVTI
     GSVEKYINDT AWDQGWVKPR TPSRELGLSV GVIGAGPAGL AAAEELRAKG YEVHVYDRYD
     RMGGLLVYGI PGFKLEKSVV ERRVKLLADA GVIYHPNFEV GRDASLPELR RKHVAVLVAT
     GVYKARDIKA PGSGLGNIVA ALDYLTTSNK VSLGDTVEAY ENGSLNAAGK HVVVLGGGDT
     AMDCVRTAIR QGATSVKCLY RRDRKNMPGS QREVAHAEEE GVEFIWQAAP EGFTGDTVVT
     GVRAVRIHLG VADATGRQTP QVIEGSEFTV QADLVIKALG FEPEDLPNAF DEPELKVTRW
     GTLLVDHRTK MTNMDGVFAA GDIVRGASLV VWAIRDGRDA AEGIHAYAKA KAEAPVAVAA
     E
//