ID D3NSB4_AZOS1 Unreviewed; 406 AA.
AC D3NSB4;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558, ECO:0000256|RuleBase:RU364075};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU364075};
DE AltName: Full=Nitrogenase metalloclusters biosynthesis protein NifS {ECO:0000256|ARBA:ARBA00031911, ECO:0000256|RuleBase:RU364075};
GN Name=nifS {ECO:0000313|EMBL:BAI71293.1};
GN Synonyms=iscS {ECO:0000313|EMBL:BAI71293.1};
GN OrderedLocusNames=AZL_006550 {ECO:0000313|EMBL:BAI71293.1};
OS Azospirillum sp. (strain B510).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI71293.1, ECO:0000313|Proteomes:UP000002040};
RN [1] {ECO:0000313|EMBL:BAI71293.1, ECO:0000313|Proteomes:UP000002040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B510 {ECO:0000313|EMBL:BAI71293.1,
RC ECO:0000313|Proteomes:UP000002040};
RX PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA Nakayama S., Yamada M., Tabata S., Sato S.;
RT "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT sp. B510.";
RL DNA Res. 17:37-50(2010).
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:0000256|ARBA:ARBA00003120}.
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:0000256|ARBA:ARBA00001357,
CC ECO:0000256|RuleBase:RU364075};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490, ECO:0000256|RuleBase:RU364075}.
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DR EMBL; AP010946; BAI71293.1; -; Genomic_DNA.
DR AlphaFoldDB; D3NSB4; -.
DR STRING; 137722.AZL_006550; -.
DR KEGG; azl:AZL_006550; -.
DR HOGENOM; CLU_003433_0_0_5; -.
DR Proteomes; UP000002040; 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 GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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 {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364075};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364075};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364075};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU364075};
KW Reference proteome {ECO:0000313|Proteomes:UP000002040};
KW Transferase {ECO:0000256|RuleBase:RU364075, ECO:0000313|EMBL:BAI71293.1}.
FT DOMAIN 10..373
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 406 AA; 43925 MW; 69664EAAD4C8A2DD CRC64;
MSRQTMNQAI YLDNNATTRV DPEVLQEMLP LFTEHFGNPS SMHGFGAAVG GKIEWARRQV
QALLGAAHDS EIVFTSGGTE SDNTAILSAL EAYPKKREII TSVVEHPGVL ALCEYLEKKR
GCTVHRIPVD GKGDLDMDAY RAALSDRVAI VSFMWANNET GTIFPVEELA RMAKEVGALF
HTDAVQSVGK IPMKLADSAI DMLSLSGHKL HAPKGIGALY VKRGLRFRPM LRGGHQERSR
RAGTENAPAI VGLGAAAQLA LVHMGEENTR VKALRDKLER AILAAVPSCF VTGNPDHRLP
NTCNIAFEYI EGEAILLLLN EAGIAASSGS ACTSGSLEPS HVMRAMGVPY TAAHGATRFS
LSRDTTEEEI DRVIAVVPGI IAKLRSLSPY WQQEAGRPKE FAPVYS
//
