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Database: UniProt
Entry: A0A1I4V3G1_9PSEU
LinkDB: A0A1I4V3G1_9PSEU
Original site: A0A1I4V3G1_9PSEU 
ID   A0A1I4V3G1_9PSEU        Unreviewed;       445 AA.
AC   A0A1I4V3G1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Selenocysteine lyase/Cysteine desulfurase {ECO:0000313|EMBL:SFM95777.1};
GN   ORFNames=SAMN05421805_1022 {ECO:0000313|EMBL:SFM95777.1};
OS   Saccharopolyspora antimicrobica.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=455193 {ECO:0000313|EMBL:SFM95777.1, ECO:0000313|Proteomes:UP000199398};
RN   [1] {ECO:0000313|EMBL:SFM95777.1, ECO:0000313|Proteomes:UP000199398}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPCC 201259 {ECO:0000313|EMBL:SFM95777.1,
RC   ECO:0000313|Proteomes:UP000199398};
RA   de Groot N.N.;
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; FOUP01000002; SFM95777.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4V3G1; -.
DR   STRING; 455193.SAMN05421805_1022; -.
DR   OrthoDB; 9804366at2; -.
DR   Proteomes; UP000199398; 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:SFM95777.1}.
FT   DOMAIN          40..408
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   445 AA;  47542 MW;  5FCBAF55BEC9D990 CRC64;
     MTSAVVSIPT QSTADYRVPA VAGSALRVPL VNGDSIGYAN LDHGASAPCL SSVQKAVDEL
     LPWYASVHRG AGFASQVCTR VYEGARDVLR EFVGARRTDS VIFTRNTTDA LNLLAKALPR
     GTSVVVFDTE HHAALLPWTG PRVRRIAAPA TPAEAVTALD AALAECPEGP RLAVLTGASN
     VTGELWPVAE LARVARRRGA RTVLDAAQLA PHRPVRITEL DVDYVAISGH KLYAPFGAGA
     LVGRADWLNA AEPYLAGGGA TRQVHERAVS WTSGAERHEA GSPNTVGVHA LAKACEELSA
     NWADVVAHEE ALLRRLRAGL REVPGLRELC LFEADRERVG VVSFTVDGQD PGLLAAALSA
     EHGIGVRDGL FCAHLATRRL LSRAGSDSDR AVRVSIGLGT TTEHVDRLVR ALRKLVAEGP
     AWRYEQVDGR WTPVDDPRPL PDFLR
//
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