ID   NIFS_CERSP              Reviewed;         387 AA.
AC   Q01179;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 92.
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   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1317839; DOI=10.1128/jb.174.12.3855-3866.1992;
RA   Meijer W.G., Tabita F.R.;
RT   "Isolation and characterization of the nifUSVW-rpoN gene cluster from
RT   Rhodobacter sphaeroides.";
RL   J. Bacteriol. 174:3855-3866(1992).
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; M86823; AAA26137.1; -; Genomic_DNA.
DR   PIR; C41880; C41880.
DR   RefSeq; WP_011338298.1; NZ_CP012960.1.
DR   AlphaFoldDB; Q01179; -.
DR   SMR; Q01179; -.
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:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
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; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR017772; Cys_deSase_NifS_bac/arc.
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.
DR   TIGRFAMs; TIGR03402; FeS_nifS; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Iron; Iron-sulfur; Metal-binding; Nitrogen fixation; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..387
FT                   /note="Cysteine desulfurase"
FT                   /id="PRO_0000150259"
FT   ACT_SITE        323
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P05341"
FT   BINDING         72..73
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         152
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O29689"
FT   BINDING         180
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         200..202
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         238
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         323
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         203
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ   SEQUENCE   387 AA;  41227 MW;  46C2F9350473C678 CRC64;
     MERVYLDNNA TTRLAPEALQ AMLPFLTEEF GNPSSLHGQG RAPARALMAA RRAVLELIGA
     EADSEILFTS GGTEADTTAI RSALAADPSR REIVTSTVEH AAVLALCDHL ERQEGVTVHR
     IPVDGDGRLD IEAYRAALSP RVALVSLMWA NNETGTVFPV EGLAELAHRA GALFHTDAVQ
     AVGKVPIVLR GTEIDMLSLS AHKFHGPKGV GALWLRKGVP FQPLIRGGRQ QRGHRAGTEN
     IPGIVGLGRA AELALGGDHG AVRLLRDRLE QGILARVPKA RVLGDPLDRL PNTSCVAFDF
     AEGEAIVMLL DRAGICVSSG AACASGAMEP SHVIRAMKVP FTAAHGAIRF SLSHWTTAAE
     IDRLLEVLPP IVDQLRALSP FGAEEVK