ID   A0A1C6MVB3_9ACTN        Unreviewed;       420 AA.
AC   A0A1C6MVB3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   ORFNames=H180DRAFT_01691 {ECO:0000313|EMBL:SCK22807.1};
OS   Streptomyces sp. WMMB 322.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1286821 {ECO:0000313|EMBL:SCK22807.1, ECO:0000313|Proteomes:UP000182082};
RN   [1] {ECO:0000313|EMBL:SCK22807.1, ECO:0000313|Proteomes:UP000182082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMMB 322 {ECO:0000313|EMBL:SCK22807.1,
RC   ECO:0000313|Proteomes:UP000182082};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily.
CC       {ECO:0000256|ARBA:ARBA00010447}.
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DR   EMBL; FMHI01000004; SCK22807.1; -; Genomic_DNA.
DR   RefSeq; WP_055485382.1; NZ_FMHI01000004.1.
DR   AlphaFoldDB; A0A1C6MVB3; -.
DR   STRING; 1286821.GCA_001418285_01687; -.
DR   Proteomes; UP000182082; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
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; IPR010970; Cys_dSase_SufS.
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   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          33..408
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   420 AA;  45853 MW;  D8F29E9D6191AD11 CRC64;
     MSNVTLPGLL DTEAIRKDFP ILDRTVHGGQ KLVYLDNAAT SQKPRQVLDA MSDYNERHNA
     NVHRGVHVLA EEATALYEGA RDKVAAFINA PSRDEVVFTK NASESLNLVA NMLGWADEPY
     RVEHDTEIVI TEMEHHSNIV PWQLLSQRTG AKLKWFGLTD DGRLDLSDVE EVITEKTKVV
     SFTLVSNIMG TINPVETIVR RAQEVGALVV VDASQAAPHM VLDVQALQAD FVAFTGHKMC
     GPTGIGVLWG RQELLDDLPP FLGGGEMIET VTMHASTYAP APHKFEAGTP PIAQAVGLGA
     AVDYLSSIGM ERIQEHEHAL TAYAVERLSR IPGLRFIGPT TAEDRGAAIS FTLGDIHPHD
     VGQVLDEQGI AVRVGHHCAR PVCLRYGIPA TTRASFYLYS MPAEVDALAE GVEHVRNFFA
//