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Database: UniProt
Entry: B4U4W5_STREM
LinkDB: B4U4W5_STREM
Original site: B4U4W5_STREM 
ID   B4U4W5_STREM            Unreviewed;       408 AA.
AC   B4U4W5;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 95.
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:ACG63032.1};
GN   OrderedLocusNames=Sez_1703 {ECO:0000313|EMBL:ACG63032.1};
OS   Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=552526 {ECO:0000313|EMBL:ACG63032.1, ECO:0000313|Proteomes:UP000001873};
RN   [1] {ECO:0000313|EMBL:ACG63032.1, ECO:0000313|Proteomes:UP000001873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGCS10565 {ECO:0000313|EMBL:ACG63032.1,
RC   ECO:0000313|Proteomes:UP000001873};
RX   PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA   Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., Deleo F.R.,
RA   Musser J.M.;
RT   "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain
RT   causing epidemic nephritis: new information about an old disease.";
RL   PLoS ONE 3:E3026-E3026(2008).
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; CP001129; ACG63032.1; -; Genomic_DNA.
DR   RefSeq; WP_012516288.1; NC_011134.1.
DR   AlphaFoldDB; B4U4W5; -.
DR   KEGG; sez:Sez_1703; -.
DR   HOGENOM; CLU_003433_2_5_9; -.
DR   Proteomes; UP000001873; 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   Transferase {ECO:0000256|RuleBase:RU004506}.
FT   DOMAIN          24..393
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   408 AA;  45117 MW;  C7AF68C388805EEA CRC64;
     MFDPNQIKAD FKLLDQYVND EALVYLDNAA TTQKPQAVLE AMQAYYQKDN ANVHRGVHTL
     AERATRQYEA SRQKVADFIG AKSSKEVIFT RGTTTSLNWV SKFAEQILKP GDEVLISIME
     HHANILPWQQ VCQKTGARLV YAYLKEGKLD MNDLQSKLGA STKFVSIAHV SNVLGCVNPI
     QEIARLAHAR GAYFVVDAAQ SVPHMAIDVQ ELDCDFLAFS GHKLLGPTGI GVLYGKEALL
     NQMNPVEFGG EMIDFVYEQE ATWKPLPWKL EAGTPHIAGA IGLGAAISYL EAIGMDQVHA
     HEADLVAYTL PRLQAIAGLT VYGPERADER SGVFAFNIDG LHPHDLATAL DYEGVAVRAG
     HHCAQPLHKY LGLHSTVRAS FYLYNTREDC DRLIEAILKA KEFFNGTF
//
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