ID W0A8C1_9SPHN Unreviewed; 380 AA.
AC W0A8C1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558};
GN ORFNames=NX02_04955 {ECO:0000313|EMBL:AHE52732.1};
OS Sphingomonas sanxanigenens DSM 19645 = NX02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1123269 {ECO:0000313|EMBL:AHE52732.1, ECO:0000313|Proteomes:UP000018851};
RN [1] {ECO:0000313|EMBL:AHE52732.1, ECO:0000313|Proteomes:UP000018851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NX02 {ECO:0000313|EMBL:AHE52732.1,
RC ECO:0000313|Proteomes:UP000018851};
RA Ma T., Huang H., Wu M., Li X., Li G.;
RT "Completed genome of Sphingomonas sanxanigenens NX02.";
RL Submitted (JUL-2013) 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. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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DR EMBL; CP006644; AHE52732.1; -; Genomic_DNA.
DR AlphaFoldDB; W0A8C1; -.
DR STRING; 1123269.NX02_04955; -.
DR KEGG; ssan:NX02_04955; -.
DR PATRIC; fig|1123269.5.peg.963; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_1_5; -.
DR Proteomes; UP000018851; 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 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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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 Reference proteome {ECO:0000313|Proteomes:UP000018851}.
FT DOMAIN 18..363
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 380 AA; 38060 MW; E4233E87501B2B2C CRC64;
MAADGEGSAG ARGMTAPVYL DYQATTPLAP EALAAMLPWL ESQHANPHSA HPPGRAARAA
VEVARDAVTA LLPAGGTLSF TGGATESLNW ALKGVGPGTI VTIATEHAAV LDTVAALAAA
GRPVTVLPVA ADGLVDLDAA RAAIVPGVAL VAAMLVNNEI GVIQPIAELA ALAHAAGALM
LCDAVQGYGR LAVPEACDLV AISAHKVHGP KGIGALWIRD GVALAPLLHG GGQEAGGRSG
TLSPALCAGF GAAARLMAER RDKDAAHVAA LWGRAREGFA DWALNGSAGA RYHGNLNMRR
AGVDVARLMS EVRGVAFSAG SACASGSGRP SHVLKAIGLA DAAARSSIRI GFGRYTTIDE
IDRAAALIGA AAERQGVQAA
//
