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Database: UniProt
Entry: A0A1N6KW71_9BURK
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Original site: A0A1N6KW71_9BURK 
ID   A0A1N6KW71_9BURK        Unreviewed;       691 AA.
AC   A0A1N6KW71;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   ORFNames=SAMN05444165_5005 {ECO:0000313|EMBL:SIO60804.1};
OS   Paraburkholderia phenazinium.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=60549 {ECO:0000313|EMBL:SIO60804.1, ECO:0000313|Proteomes:UP000185151};
RN   [1] {ECO:0000313|EMBL:SIO60804.1, ECO:0000313|Proteomes:UP000185151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAS95 {ECO:0000313|EMBL:SIO60804.1,
RC   ECO:0000313|Proteomes:UP000185151};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FSRU01000002; SIO60804.1; -; Genomic_DNA.
DR   RefSeq; WP_074300063.1; NZ_FSRU01000002.1.
DR   AlphaFoldDB; A0A1N6KW71; -.
DR   OrthoDB; 9808002at2; -.
DR   Proteomes; UP000185151; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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; NF041166; f2_encap_cargo1; 1.
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   Lyase {ECO:0000313|EMBL:SIO60804.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185151}.
FT   DOMAIN          311..680
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   691 AA;  71750 MW;  AD0C3BEE044F6DC0 CRC64;
     MTIQTPTSNP LAGGVPHDVP QTLPAGLPDP ATLARLATEF FAALPGGGVS SAAPGGSLTD
     AASSASFASA LPVAAPGLSS VSNPAPPGSP LAGPGGFGTG VPGAALPQGK VAGANLLPSA
     PTHVLSLGNR APALVPHAAA QNGLPDSAVT IAPALEPRFG GAALGVPEGL GAQRPSAGGA
     SGAPAAASPY YFLNEQAGTP GNGPSGSRDI VVPSSDTVTA QSFGLPGEAE LRSLLSVQRF
     PYDAPSRDAA TTDRSGVSRY FVDEAQASAG PSRAAHAVPN AAASAHPPFD VNAIRRDFPI
     LSERVNGRQL VWFDNAATTH KPQSVIDRLA YFYAHENSNI HRAAHALAGR ATDAYEAARS
     KVQRFIGAAS PDEIVFVRGT TEAINLIAKS WGVQNVGEGD EIIVSNLEHH ANIVPWQQLA
     AQTGAKLRVI PVDDSGQVLL DEYRKLLNDR TRIVSVTQVS NALGTVVPVK EIVEMAHRAG
     AKALVDGAQS VSHMRVDVQA IDADFFVFSG HKVFGPTGIG VVYGKRAILE DMPPWQGGGN
     MIADVTFERT VFQPPPNRFE AGTGNIADAV GLGAALDYVT RIGIENIARY EHDLLAYATS
     VLQPVPGVRL IGTAKDKASV LSFVLKGYET EEVGQALNEE GIAVRSGHHC AQPILRRFGV
     EATVRPSLAF YNTCDEVDAL VSVVRRLSTR R
//
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