ID A0A133Q8J5_STALU Unreviewed; 413 AA.
AC A0A133Q8J5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|RuleBase:RU004506};
DE EC=2.8.1.7 {ECO:0000256|RuleBase:RU004506};
GN ORFNames=HMPREF3225_00843 {ECO:0000313|EMBL:KXA39212.1};
OS Staphylococcus lugdunensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=28035 {ECO:0000313|EMBL:KXA39212.1, ECO:0000313|Proteomes:UP000070063};
RN [1] {ECO:0000313|EMBL:KXA39212.1, ECO:0000313|Proteomes:UP000070063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJR7738 {ECO:0000313|EMBL:KXA39212.1,
RC ECO:0000313|Proteomes:UP000070063};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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|ARBA:ARBA00002824,
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXA39212.1}.
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DR EMBL; LRQI01000029; KXA39212.1; -; Genomic_DNA.
DR RefSeq; WP_060795373.1; NZ_KQ957371.1.
DR AlphaFoldDB; A0A133Q8J5; -.
DR STRING; 28035.B6N84_09900; -.
DR PATRIC; fig|28035.7.peg.854; -.
DR eggNOG; COG0520; Bacteria.
DR Proteomes; UP000070063; Unassembled WGS sequence.
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 29..398
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 413 AA; 46017 MW; B8FB40CEA7FC9AB9 CRC64;
MADTTLNVED VIKDFPILQQ QVNGKRLAYL DSTATSQKPI QVLNVLDDYY KRYNSNVHRG
VHTLGSLATD GYESARETVR RFINAHYFEE VVFTRGTTAS INMIAHSYGD AHVEAGDEIV
VTEMEHHANI VPWQQLAKRK QATLKFIPMT AEGELRVEDI KATITDKTKI VAITHVSNVL
GTINDVKMIA KIAHEHGAII SVDGAQSAPH MPIDVQDLDC DFFSFSGHKM LGPTGIGVLY
GKRDLLNDME PVEFGGDMID FVSKYDATWA DLPTKFEAGT PLIAQAIGLA EAIRYIENIG
FEAIHRHERA LTKYAYEQMS AIEGIDIYGP PKDRRAGVIT FNLKDVHPHD VATAVDTEGV
AVRAGHHCAQ PLMSWLNVSS TARASFYIYN TQQDVDQLVN ALKQTKEFFS YEF
//
