ID   NIFS_ALKHC              Reviewed;         375 AA.
AC   Q9KDJ6;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Putative cysteine desulfurase NifS {ECO:0000305};
DE            EC=2.8.1.7 {ECO:0000250|UniProtKB:P05341};
GN   Name=nifS; Synonyms=iscS; OrderedLocusNames=BH1217;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to
CC       produce alanine. {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   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000004; BAB04936.1; -; Genomic_DNA.
DR   PIR; A83802; A83802.
DR   RefSeq; WP_010897385.1; NC_002570.2.
DR   AlphaFoldDB; Q9KDJ6; -.
DR   SMR; Q9KDJ6; -.
DR   STRING; 272558.10173833; -.
DR   EnsemblBacteria; BAB04936; BAB04936; BAB04936.
DR   KEGG; bha:BH1217; -.
DR   eggNOG; COG1104; Bacteria.
DR   HOGENOM; CLU_003433_0_0_9; -.
DR   OMA; CLQSANH; -.
DR   OrthoDB; 839689at2; -.
DR   Proteomes; UP000001258; Chromosome.
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   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; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..375
FT                   /note="Putative cysteine desulfurase NifS"
FT                   /id="PRO_0000150285"
FT   ACT_SITE        319
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P05341"
FT   BINDING         69..70
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         177
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         195..197
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         233
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         319
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         198
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ   SEQUENCE   375 AA;  41934 MW;  FE7228B89716560A CRC64;
     MIYLDYCATT PMSDYVKDVY VTVASQFYGN PNSLHDVGYE ASNILEQCKR QIANLLHIDP
     AGIFFTGSAS EANFLTIVSL ALAHRRKGRH LITTKCEHPS VLSTFRYLES QQFDVSYVPV
     NRYGQVSVDA LMGTIREDTI LVSIAHSQSV LGTIQSLETF AEPLVTYDIL FHSDCTQSIG
     KVDVPIRQLH SLTMSGHKIN GPKGIGLAYV DPAIQWEPFL SGVTQQSGFR QGTVDIPSVA
     AFTAAIEESF QHRTAYDQHI TKLHHQFKEK MMEWPMILEG HPSNRLKHHF GLRLHGMEGQ
     FVMLEANRAG FAISTGTACS SSHHEPDPVF AAIGRTKEEA DQFFRVSFGI STTEQEFNAF
     IDFLQQLIDR KGEPM