ID   NIFS_ENTAG              Reviewed;         401 AA.
AC   Q52069;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
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   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OG   Plasmid pEA3.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=333;
RA   Steibl H.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
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; X99694; CAA68020.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q52069; -.
DR   SMR; Q52069; -.
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; Plasmid;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..401
FT                   /note="Cysteine desulfurase"
FT                   /id="PRO_0000150254"
FT   ACT_SITE        324
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         151
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O29689"
FT   BINDING         179
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         199..201
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         237
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         324
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         202
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ   SEQUENCE   401 AA;  43874 MW;  3584D655FDC3F5D0 CRC64;
     MKNVYLDNNA TTRIDPMVLE AMMPYLRDYY GNPSSIHDFG GPCRAGLECA REQVASLLGA
     AYTSEIIFTS CATEATSTAI YSAIALAPER REIITTAVEH PATLAVCEHL ERQGYMIHRI
     GVSEEGALDT AHYYDALSEN VALVTMMWAN NETGVLFPVS EMATAAHERG ILFHCDAVQA
     VGKIPISLRA TDIDMLSCSA HKIHGPKGCG CLYLRRNTRF RPLVRGGHQE RGRRAGTENI
     AGIVGMGAAC ELADVHMPMM ASVQEMRDRL ETGLLTTIPH TLLMGANQPR TPNTVNIAFE
     YIEGEAILLL LNHCGIAASS GSACTSGSLE PSHVMRAMNI PYTAAHGSIR FSLSRFTRER
     EIEWAIEQMP DIVARLRTLS PYWQQDKVQI AQGGLFAPTY G