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Database: UniProt
Entry: A0A0X1RYY9_9BACL
LinkDB: A0A0X1RYY9_9BACL
Original site: A0A0X1RYY9_9BACL 
ID   A0A0X1RYY9_9BACL        Unreviewed;       408 AA.
AC   A0A0X1RYY9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   Name=sufS {ECO:0000313|EMBL:AMA63736.1};
GN   ORFNames=ASO14_685 {ECO:0000313|EMBL:AMA63736.1};
OS   Kurthia sp. 11kri321.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX   NCBI_TaxID=1750719 {ECO:0000313|EMBL:AMA63736.1, ECO:0000313|Proteomes:UP000058129};
RN   [1] {ECO:0000313|EMBL:AMA63736.1, ECO:0000313|Proteomes:UP000058129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11kri321 {ECO:0000313|EMBL:AMA63736.1,
RC   ECO:0000313|Proteomes:UP000058129};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-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; CP013217; AMA63736.1; -; Genomic_DNA.
DR   RefSeq; WP_068451438.1; NZ_CP013217.1.
DR   AlphaFoldDB; A0A0X1RYY9; -.
DR   STRING; 1750719.ASO14_685; -.
DR   KEGG; kur:ASO14_685; -.
DR   PATRIC; fig|1750719.3.peg.646; -.
DR   OrthoDB; 9804366at2; -.
DR   Proteomes; UP000058129; 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:SF8; 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|RuleBase:RU004506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000058129};
KW   Transferase {ECO:0000256|RuleBase:RU004506}.
FT   DOMAIN          23..394
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   408 AA;  44908 MW;  4D9140257DFCC350 CRC64;
     MIKDDIRSYF PILNQEINGN PLIYLDSAAT SQKPIQVIES LKKYYEFDNS NVHRGVHTLG
     NRATDEYEGA REKVRQFINA KSTEEIIFTR GTTTGLNMVA SSYGRANVSE GDEIVITYME
     HHSNLIPWQQ LAKATKATLK YIELEADGTL SMDEVKKAIT DRTKIVAITM ASNVLGTIND
     VKAIAQVAHQ HDAVMVVDGA QGVPHMKTDV QDLDCDFLAF SGHKMCGPTG IGVLYGKKEH
     LLNMEPVEFG GEMINFVGLQ DSTWADLPAK FEAGTPIIAG AIGLGAAIDF LNEIGMDEII
     AHEHKLAKYA FENLSTVEGL TIYGPQNPEI RTGLVTFNID DVHPHDLATA LDSNGIAVRA
     GHHCAQPLMK WLNCVATARA SFYLYNDEAD IDELTKGVRF AKEYFANV
//
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