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Database: UniProt
Entry: A0A0P0DKC5_9CAUL
LinkDB: A0A0P0DKC5_9CAUL
Original site: A0A0P0DKC5_9CAUL 
ID   A0A0P0DKC5_9CAUL        Unreviewed;       379 AA.
AC   A0A0P0DKC5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558};
GN   ORFNames=JL11_10450 {ECO:0000313|EMBL:ALJ08717.1};
OS   Brevundimonas sp. DS20.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1532555 {ECO:0000313|EMBL:ALJ08717.1, ECO:0000313|Proteomes:UP000059212};
RN   [1] {ECO:0000313|EMBL:ALJ08717.1, ECO:0000313|Proteomes:UP000059212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS20 {ECO:0000313|EMBL:ALJ08717.1,
RC   ECO:0000313|Proteomes:UP000059212};
RA   Scott D., Ely B.;
RT   "Conservation of the essential genome among Caulobacter and Brevundimonas
RT   species.";
RL   Submitted (OCT-2015) 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. NifS/IscS subfamily.
CC       {ECO:0000256|ARBA:ARBA00006490}.
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DR   EMBL; CP012897; ALJ08717.1; -; Genomic_DNA.
DR   RefSeq; WP_054765623.1; NZ_CP012897.1.
DR   AlphaFoldDB; A0A0P0DKC5; -.
DR   STRING; 1532555.JL11_10450; -.
DR   KEGG; brd:JL11_10450; -.
DR   Proteomes; UP000059212; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.260.50; -; 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; IPR016454; Cysteine_dSase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Aminotransferase {ECO:0000313|EMBL:ALJ08717.1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000313|EMBL:ALJ08717.1}.
FT   DOMAIN          4..349
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   379 AA;  38366 MW;  32F1ED9EB39FFE0B CRC64;
     MSAVYLDYNA SGLVRPEVLE IMTQALADNG NPSAVHAAGR RARARIETAR AQVAELVGAD
     PTAVVFNSGG TEANAQAIAS ALAAGCERLI VSATEHPCVA EAAAAAGAPV EILPVDANGL
     VDLAWLAEAL ARPGRAVVAI HHANNESGVI QPIAQAAALV RAAGGWLHVD AIQSAGKIAV
     DIRALDADSL TLSAHKLGGP QGVGALVFKE GVSGVRILHG AGQERGLRAG TENGPGIAGF
     GVAAVCAARD LETVASHAAW RDAAQARVKA AGATIIGEGA DRLPNTLFLA VEGWDSPQQL
     ITLDLAGIMV SAGSACSSGK VKPSKTISAM GLNGLATGGV RVSGGWGTTE GDWARFADAW
     VDAWTKHKAR AAARVREVA
//
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