ID   NIFS_AZOBR     STANDARD;      PRT;   398 AA.
AC   P70727;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Cysteine desulfurase (EC 2.8.1.7) (Nitrogenase metalloclusters
DE   biosynthesis protein nifS).
GN   Name=nifS;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=98164354; PubMed=9503607;
RA   Frazzon J.S., Schrank I.S.;
RT   "Sequencing and complementation analysis of the nifUSV genes from
RT   Azospirillum brasilense.";
RL   FEMS Microbiol. Lett. 159:151-158(1998).
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur atoms from
CC       cysteine to produce alanine. Seems to participate in the
CC       biosynthesis of the nitrogenase metalloclusters by providing the
CC       inorganic sulfur required for the Fe-S core formation (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: L-cysteine + [enzyme]-cysteine = L-alanine +
CC       [enzyme]-S-sulfanylcysteine.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/iscS subfamily.
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; U26427; AAC46177.1; -.
DR   HSSP; P39171; 1P3W.
DR   InterPro; IPR000192; Aminotrans_V.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; FALSE_NEG.
KW   Nitrogen fixation; Pyridoxal phosphate; Transferase.
FT   BINDING     205    205       Pyridoxal phosphate (covalent) (By
FT                                similarity).
FT   ACT_SITE    327    327       By similarity.
SQ   SEQUENCE   398 AA;  42426 MW;  A0437F6D485181A5 CRC64;
     MTAQGIYLDN NATTRVDPDV LAEMLPLFTE QFGNPSSMHG FGAAVGGQDR MGAQAGAGAA
     RAAHDSEIVF TSGGTESDNT AILSTLEAYP KKKSIVTSVV EHPAVLALCD YLEKKRGYTV
     HRIGVDNRGN LDLDAYKRCA LGPDVAIVSI MWANNETGTI FPIEELAQLA KAAGAVFHTA
     VQAVGKIPMN VRHSAVDMLC ACGHKLHAPK GVHALYVKRG LRFRPIVRGG HQERSRRAGN
     GERAGHRRAG GGAHVALMHM TDENTRVKRS RQAGAAILAA VPNCFVTGNP ANRLPNTCNV
     AFEYIEGEAI LLLLNEADIA ASSGSACTSG SLEPSHVMRA MGVPYTAAHG PTRLSLSRET
     TEEEIDRVIR VVPGMRTGRS VSPYWSQAAP EGVRPVYS
//