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Database: UniProt
Entry: A0A1C4VQL0_9ACTN
LinkDB: A0A1C4VQL0_9ACTN
Original site: A0A1C4VQL0_9ACTN 
ID   A0A1C4VQL0_9ACTN        Unreviewed;       434 AA.
AC   A0A1C4VQL0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   ORFNames=GA0070612_1697 {ECO:0000313|EMBL:SCE86302.1};
OS   Micromonospora chokoriensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=356851 {ECO:0000313|EMBL:SCE86302.1, ECO:0000313|Proteomes:UP000198224};
RN   [1] {ECO:0000313|EMBL:SCE86302.1, ECO:0000313|Proteomes:UP000198224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45160 {ECO:0000313|EMBL:SCE86302.1,
RC   ECO:0000313|Proteomes:UP000198224};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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; LT607409; SCE86302.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4VQL0; -.
DR   eggNOG; COG0520; Bacteria.
DR   Proteomes; UP000198224; Chromosome i.
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:SF27; 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:SCE86302.1}.
FT   DOMAIN          44..426
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  44772 MW;  EB2A4B4B3F7A5ADD CRC64;
     MPVTLLPSLP TRVDAAPEPA ATEPAAPEPA SSGPLDVLGV PGEINLDYAA SAPCARAAAD
     AVAELLPWYA SVHRGAGALS RRCTLAYEQA RQTVGDAFGA RVDDHVFFTR NTTDALNLLA
     RALPAGTTVV TFAGEHHANL LPWPRGSVRL PVPTDPDAAV RDLAAALTEL RRGSNPALPV
     LVAVTGASNV TGELWPVTEL ARVAHRHGAR IVLDAAQLAP HAPVDLLALD VDYLAVSGHK
     LYAPFGAGVL IGRADWLDAA PPYLAGGGAT SHVGPATHDV NWATGPARHE GGTPNLLGAV
     ALAAVCTALD DADRAALAAH EQALLTRLRT GIAALPHVVE LRTFGPDAPR VGIVSFVVVG
     WDSSAVAARL AAEHHIGVRD GLFCAHPLAR RLLSEAAGRT GRRDLPSTAL RASIGLGTTE
     AQVDKLLAAL ADLG
//
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