ID NIFS_AZOCH Reviewed; 396 AA.
AC P23120;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 89.
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 Azotobacter chroococcum mcd 1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1885524; DOI=10.1128/jb.173.17.5457-5469.1991;
RA Evans D.J., Jones R., Woodley P.R., Wilborn J.R., Robson R.L.;
RT "Nucleotide sequence and genetic analysis of the Azotobacter chroococcum
RT nifUSVWZM gene cluster, including a new gene (nifP) which encodes a serine
RT acetyltransferase.";
RL J. Bacteriol. 173:5457-5469(1991).
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; M60090; AAA22160.1; -; Genomic_DNA.
DR PIR; B43706; B43706.
DR AlphaFoldDB; P23120; -.
DR SMR; P23120; -.
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:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.260.50; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR03402; FeS_nifS; 1.
DR PANTHER; PTHR11601:SF63; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..396
FT /note="Cysteine desulfurase"
FT /id="PRO_0000150251"
FT ACT_SITE 319
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:P05341"
FT BINDING 71..72
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 148
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT BINDING 176
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 196..198
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 231
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 199
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ SEQUENCE 396 AA; 43296 MW; 188FCD056EB453FC CRC64;
MADVYLDNNA TTRVDDEIVE AMLPFFTEQF GNPSSLHSFG NQVGLALKRA RQQRAGVLGE
HDSEIIFTSC GTESDHAILS ALSPARAQDL ITTVVEHPAV LSLCDYLASE GYTVHKLPVD
KKGRLDLDHY ASLLNDDVAV VSVMWANNET GTLFPVEEMA RMADEAGIMF HTDAVQAVRK
LPIDLKNSSI HMLSLSGHKL HRKGVGVLYL RRGTRFRRCC RGHQERPAGG TENAASIIAM
GWAAERALAF MEHENTEVKR LRDKLEAGIL AVVPHAFVTG DPDNRLPNTA NIAFEYIEGE
AILLLLNKVG IAASSGSACT SGSLEPSHVM RAMDIPYTAA HGTVRFSLSR YTTEEEIDRV
IREVPPIVAQ LRNVSPYWSG NGPVEHPGKA FAPVYG
//
