ID A0A085TS09_9RHOB Unreviewed; 406 AA.
AC A0A085TS09;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=DW2_17557 {ECO:0000313|EMBL:KFE33506.1};
OS Thioclava atlantica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1317124 {ECO:0000313|EMBL:KFE33506.1, ECO:0000313|Proteomes:UP000028607};
RN [1] {ECO:0000313|Proteomes:UP000028607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13D2W-2 {ECO:0000313|Proteomes:UP000028607};
RA Lai Q., Li G., Shao Z.;
RT "Thioclava sp. 13D2W-2 Genome Sequencing.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFE33506.1, ECO:0000313|Proteomes:UP000028607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13D2W-2 {ECO:0000313|EMBL:KFE33506.1,
RC ECO:0000313|Proteomes:UP000028607};
RX PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
RA Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
RT "Thioclava indica sp. nov., isolated from surface seawater of the Indian
RT Ocean.";
RL Antonie Van Leeuwenhoek 107:297-304(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFE33506.1}.
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DR EMBL; AQRC01000018; KFE33506.1; -; Genomic_DNA.
DR RefSeq; WP_038148547.1; NZ_AQRC01000018.1.
DR AlphaFoldDB; A0A085TS09; -.
DR STRING; 1317124.DW2_17557; -.
DR PATRIC; fig|1317124.6.peg.3536; -.
DR eggNOG; COG0520; Bacteria.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000028607; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
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; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 24..394
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 406 AA; 44330 MW; EF7D5685B43DC00A CRC64;
MYDIQKIRAD FPILSREVNG KPLVYLDNGA SAQKPRVVID AMTRMYEEDY SNVHRGLHTL
SNIATEKYEG VRGIVARFLG VKDAEEIVFT TGSTEGINLV SYAWAAPRLQ AGDEIVLSVL
EHHANIVPWH FLRERQGVKL VWVEPEADGS LPAEKVLEAV TDRTRLIAIT HMSNVLGTKV
DVKAIAHAAR EKGIATLVDG SQGAVHGPVD LDDIGADFYA ITGHKLYGPS GSGAIHIRRE
RMEEMRPFLG GGDMIDTVTR DSVTYNKPPM KFEAGTPGIV QQVGMGVALD YLMQVGMENI
AAHERDLRDY AQQKLSGLNW LNLQGSAPDK GAIFSLTLNG PAHPHDISTI LDKRGVAVRA
GSHCAMPLMD WLGVSATARA SFGMYNTREE VDALVSALEL CHELLG
//
