ID   NIFS_AZOBR              Reviewed;         398 AA.
AC   P70727;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Cysteine desulfurase {ECO:0000250|UniProtKB:P05341};
DE            EC=2.8.1.7 {ECO:0000250|UniProtKB:P05341};
DE   AltName: Full=Nitrogenase metalloclusters biosynthesis protein NifS {ECO:0000250|UniProtKB:P05341};
GN   Name=nifS {ECO:0000250|UniProtKB:P05341};
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9503607; DOI=10.1111/j.1574-6968.1998.tb12854.x;
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 cysteine
CC       to produce alanine. Seems to participate in the biosynthesis of the
CC       nitrogenase metalloclusters by providing the inorganic sulfur required
CC       for the Fe-S core formation. {ECO:0000250|UniProtKB:P05341}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC         alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC         COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:64428; EC=2.8.1.7;
CC         Evidence={ECO:0000250|UniProtKB:P05341};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P05341};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P05341}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
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DR   EMBL; U26427; AAC46177.1; -; Genomic_DNA.
DR   AlphaFoldDB; P70727; -.
DR   SMR; P70727; -.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR016454; Cysteine_dSase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Iron; Iron-sulfur; Metal-binding; Nitrogen fixation; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..398
FT                   /note="Cysteine desulfurase"
FT                   /id="PRO_0000150250"
FT   REGION          230..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        327
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P05341"
FT   BINDING         74..75
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         155
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O29689"
FT   BINDING         182
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         202..204
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         327
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /note="via persulfide group"
FT                   /evidence="ECO:0000250|UniProtKB:O29689"
FT   MOD_RES         205
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
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