ID   A0A0C5W282_9GAMM        Unreviewed;       405 AA.
AC   A0A0C5W282;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=YC6258_04732 {ECO:0000313|EMBL:AJQ96764.1};
OS   Gynuella sunshinyii YC6258.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Saccharospirillaceae; Gynuella.
OX   NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ96764.1, ECO:0000313|Proteomes:UP000032266};
RN   [1] {ECO:0000313|EMBL:AJQ96764.1, ECO:0000313|Proteomes:UP000032266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC6258 {ECO:0000313|EMBL:AJQ96764.1,
RC   ECO:0000313|Proteomes:UP000032266};
RA   Khan H., Chung E.J., Chung Y.R.;
RT   "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT   YC6258T gen. nov., sp. nov.";
RL   Submitted (JAN-2014) 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; CP007142; AJQ96764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C5W282; -.
DR   STRING; 1445510.YC6258_04732; -.
DR   KEGG; gsn:YC6258_04732; -.
DR   PATRIC; fig|1445510.3.peg.4694; -.
DR   HOGENOM; CLU_003433_2_5_6; -.
DR   OrthoDB; 9808002at2; -.
DR   Proteomes; UP000032266; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   Lyase {ECO:0000313|EMBL:AJQ96764.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032266};
KW   Transferase {ECO:0000256|RuleBase:RU004506, ECO:0000313|EMBL:AJQ96764.1}.
FT   DOMAIN          24..394
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   405 AA;  44712 MW;  BC67E5C7C39FA9B1 CRC64;
     MFNVDEVRAD FPILEQQVNG QPLVYLDNAA TTQKPNQVID ALSDYYRCDN ANVHRGAHTL
     SDRSTHKFEA AREKVRDFIR AAHSHEIIWT KGTTESINLV AYCYGSMVLE EGDTVLVSAM
     EHHSNIVPWQ LVAARKNAQV LPIPVSDKGE MAIETLETML QQHSVKMVAI AHVSNALGTI
     NPIREVIDLA HRHGAKVLVD GAQGISHWPV DVQKLDVDFY AFSGHKMFAP TGIGVLYGKE
     ELLNAMPPFL GGGEMIETVS FAGTTFNQLP FKFEAGTPNI ADVIGLGAAI DYLEQFDRQQ
     LIDHELDILN YAFKRAEECQ GINVVGQAQH RAGVLSFNLQ GAHPSDVGML LDQQGVAVRT
     GHHCAQPIMA QLGIPGTVRA SFSIYNHRQD IDRLFAALEK VKQFL
//