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
//