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Database: UniProt
Entry: A0A0D5NLS6_9BACL
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ID   A0A0D5NLS6_9BACL        Unreviewed;       408 AA.
AC   A0A0D5NLS6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
GN   ORFNames=VN24_17100 {ECO:0000313|EMBL:AJY75957.1};
OS   Paenibacillus beijingensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1126833 {ECO:0000313|EMBL:AJY75957.1, ECO:0000313|Proteomes:UP000032633};
RN   [1] {ECO:0000313|EMBL:AJY75957.1, ECO:0000313|Proteomes:UP000032633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24997 {ECO:0000313|EMBL:AJY75957.1,
RC   ECO:0000313|Proteomes:UP000032633};
RX   PubMed=25937453; DOI=10.1016/j.jbiotec.2015.04.015;
RA   Kwak Y., Shin J.H.;
RT   "Complete genome sequence of Paenibacillus beijingensis 7188(T) (=DSM
RT   24997(T)), a novel rhizobacterium from jujube garden soil.";
RL   J. Biotechnol. 206:75-76(2015).
RN   [2] {ECO:0000313|Proteomes:UP000032633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24997 {ECO:0000313|Proteomes:UP000032633};
RA   Kwak Y., Shin J.-H.;
RT   "Genome sequence of Paenibacillus beijingensis strain DSM 24997T.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms
CC       from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to
CC       produce L-alanine. {ECO:0000256|RuleBase:RU004506}.
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:RU004506};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004504};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily. {ECO:0000256|ARBA:ARBA00010447,
CC       ECO:0000256|RuleBase:RU004506}.
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DR   EMBL; CP011058; AJY75957.1; -; Genomic_DNA.
DR   RefSeq; WP_045671385.1; NZ_CP011058.1.
DR   AlphaFoldDB; A0A0D5NLS6; -.
DR   STRING; 1126833.VN24_17100; -.
DR   KEGG; pbj:VN24_17100; -.
DR   PATRIC; fig|1126833.4.peg.3751; -.
DR   HOGENOM; CLU_003433_2_5_9; -.
DR   OrthoDB; 9804366at2; -.
DR   Proteomes; UP000032633; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06453; SufS_like; 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; IPR010970; Cys_dSase_SufS.
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; TIGR01979; sufS; 1.
DR   PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR   PANTHER; PTHR43586:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032633};
KW   Transferase {ECO:0000256|RuleBase:RU004506}.
FT   DOMAIN          23..392
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   408 AA;  44596 MW;  D4C5FE4E8C6C542B CRC64;
     MNIQGIREQF PILHQEINGH PLVYLDSAAT SQKPRSVIEA VKRYYELDNA NVHRGVHTLG
     SRATDAYEGA RARVAEFLNA AGPEQIVFTR GTTGALNLVA SSYAPSVLQE GDEIVITPME
     HHSNLIPWQQ AARRSGAVLK YIPLQPDGTI SLEDVERTVT DKTKIVSVTY VSNVLGTINP
     VKEIAAIAHR SGAVIVVDGA QSTPHMRIDV QDLDLDFYAL SGHKMCGPTG IGALYGRKSL
     LEAMEPVEFG GEMIDHVDLY ESTWKEIPWR FEGGTPIIAG AVGLAAAIDF LEEIGLDTID
     AHERQLASYA YDKLSAIDGL TIYGPKQNRV GLVTFNLDDI HPHDVATVLD SEGVAVRAGH
     HCCQPLMRWL DVTATARASF YLYNTEEDVD RLAASLLKTK EFFGHAIG
//
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