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Database: UniProt
Entry: A0A1I6YRV1_9ACTN
LinkDB: A0A1I6YRV1_9ACTN
Original site: A0A1I6YRV1_9ACTN 
ID   A0A1I6YRV1_9ACTN        Unreviewed;       448 AA.
AC   A0A1I6YRV1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Selenocysteine lyase/Cysteine desulfurase {ECO:0000313|EMBL:SFT53195.1};
GN   ORFNames=SAMN05660657_01396 {ECO:0000313|EMBL:SFT53195.1};
OS   Geodermatophilus amargosae.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1296565 {ECO:0000313|EMBL:SFT53195.1, ECO:0000313|Proteomes:UP000199546};
RN   [1] {ECO:0000313|Proteomes:UP000199546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46136 {ECO:0000313|Proteomes:UP000199546};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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         ECO:0000256|RuleBase:RU004504};
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; FPBA01000003; SFT53195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6YRV1; -.
DR   STRING; 1296565.SAMN05660657_01396; -.
DR   Proteomes; UP000199546; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR   PANTHER; PTHR43586:SF8; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:SFT53195.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199546}.
FT   DOMAIN          35..405
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   REGION          429..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  47329 MW;  0F74D0AB0E964DE4 CRC64;
     MTSSSGTGTL PRRDHLVGAD LHVPVAGEPR RYVDLDAAAT TSASEAVVRA VEEFLPWYSS
     VHRGAGAKSQ VSSARYEQAR ETLVRFVGAD PATHVALFPR NTTEGLNLIA FRLGLTRDDV
     VVTTAVEHHA NLLPWRRHAR LRVVDVDQSG TFDVAAVVAA LDERPTPRVL AVSGASNVTG
     WLPDLAALAA AARDRGVLVV VDGAQLVPHR QVEMAALGID VLAWSGHKMF APFGAGGLVL
     GRRLLADGEP FLVGGGSVKA VSYEEVVWAD TPDRDDAGSP NVVGVVALAA AAEELRAGRE
     RNRIQEEALV RALDDELATV PGLRRLGPTS GDRLPVAAFV IDGVHHGEVA ARLAREHGIG
     VRSGCFCAHP YIGRLLALTR SEVEQFHEDA RADLHDRLPG AVRVSCSSAT PLADVAVLGE
     ALRGIAGPLP GRRPSPACSD DRSAPVVT
//
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