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Database: UniProt
Entry: A0A0P1I6P3_9RHOB
LinkDB: A0A0P1I6P3_9RHOB
Original site: A0A0P1I6P3_9RHOB 
ID   A0A0P1I6P3_9RHOB        Unreviewed;       348 AA.
AC   A0A0P1I6P3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558};
GN   Name=iscS {ECO:0000313|EMBL:CUJ93580.1};
GN   ORFNames=PH7735_01637 {ECO:0000313|EMBL:CUJ93580.1};
OS   Shimia thalassica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=1715693 {ECO:0000313|EMBL:CUJ93580.1, ECO:0000313|Proteomes:UP000051870};
RN   [1] {ECO:0000313|Proteomes:UP000051870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7735 {ECO:0000313|Proteomes:UP000051870};
RA   Rodrigo-Torres Lidia, Arahal R.David.;
RL   Submitted (SEP-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; CYTW01000001; CUJ93580.1; -; Genomic_DNA.
DR   RefSeq; WP_058310746.1; NZ_CYTW01000001.1.
DR   AlphaFoldDB; A0A0P1I6P3; -.
DR   STRING; 1715693.PH7735_01637; -.
DR   GeneID; 83880688; -.
DR   Proteomes; UP000051870; Unassembled WGS sequence.
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; 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; 2.
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   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:UP000051870};
KW   Transferase {ECO:0000313|EMBL:CUJ93580.1}.
FT   DOMAIN          5..80
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   DOMAIN          122..329
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   348 AA;  36171 MW;  EE060F98167C7A2C CRC64;
     MKPRVYLDHN ATTPLRAEAR AAMTDAMDVI GNPSSVHAEG RKAKSVLERA RADVTTAFGA
     DGADVIFTAT ATEAAALALR DRAFHAGDIE HDAVAAWVTS DLSVGLDGAV TVTEPAQTVL
     QAANSETGIV QKLPEGLAVS DMTQAFGKLP VAFNWSGCQM AMISAHKLGG PKGIGALVVK
     RGTDIEAQIR GGGQEMGRRS GTENIIGAAG FAAAAKAAAD DLANGVWDRV ASLRDLLEET
     LVAEADDTIF VGAGVDRLPN TLCLATPGWK GETQVMQMDL AGYAISAGSA CSSGKVRASR
     VLKAMGYAEE IAAGAIRVSL GPESTEQDVL GFAESWLAHY RKHRARAA
//
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