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Database: UniProt
Entry: A0A1G8V0H3_9PSED
LinkDB: A0A1G8V0H3_9PSED
Original site: A0A1G8V0H3_9PSED 
ID   A0A1G8V0H3_9PSED        Unreviewed;       401 AA.
AC   A0A1G8V0H3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   ORFNames=SAMN05216186_10257 {ECO:0000313|EMBL:SDJ59571.1};
OS   Pseudomonas indica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=137658 {ECO:0000313|EMBL:SDJ59571.1, ECO:0000313|Proteomes:UP000198706};
RN   [1] {ECO:0000313|EMBL:SDJ59571.1, ECO:0000313|Proteomes:UP000198706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21544 {ECO:0000313|EMBL:SDJ59571.1,
RC   ECO:0000313|Proteomes:UP000198706};
RA   de Groot N.N.;
RL   Submitted (OCT-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         ECO:0000256|RuleBase:RU004504};
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; FNFD01000002; SDJ59571.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8V0H3; -.
DR   STRING; 137658.SAMN05216186_10257; -.
DR   Proteomes; UP000198706; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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   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.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198706}.
FT   DOMAIN          23..389
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   401 AA;  43026 MW;  BB97DB770EE0871E CRC64;
     MALDSPWRSD FPALAAFEAE GQVYLDSAAT AQKPQAVLDA LLGYYTSGAA NVHRAQHLPG
     ERATRAFEAT RTKATHWLNA HSPAEIVFTR GATEAFNLLA YGLEAEFEAG DEIVISALEH
     HANLLPWQQL ALRRGLRLLV LPLTAEGVVD MDAARELIGP QTRLLAISQL SNVLGCWQPL
     TELIALAKVH DALTVVDGAQ GVVHGRHDVQ VLGCDFYVFS SHKLYGPEGV GVLYGRSEAL
     QRLRHWQFGG EMVHLADYHS ADFHGAPMGF EAGTPPIGGV IALGAALDYL GSLDTGALFA
     HEAVLHGKLL AGLKVRDGVR VLGTPQAALA SFVVDGVHTA DLAHLLGEQG IAVRAGQHCA
     MPLYKRLGLT GAIRVSLGLY NDTADLDHFF TALDRALELL R
//
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