ID A0A0P8E3P3_9EURY Unreviewed; 410 AA.
AC A0A0P8E3P3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=MPEBLZ_00257 {ECO:0000313|EMBL:KPQ45174.1};
OS Candidatus Methanoperedens sp. BLZ1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX NCBI_TaxID=1719120 {ECO:0000313|EMBL:KPQ45174.1, ECO:0000313|Proteomes:UP000050360};
RN [1] {ECO:0000313|EMBL:KPQ45174.1, ECO:0000313|Proteomes:UP000050360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Arshad A., Speth D.R., De Graaf R.M., Op Den Camp H.J., Jetten M.S.,
RA Welte C.U.;
RT "A metagenomics-based metabolic model of nitrate-dependent anaerobic
RT oxidation of methane by Methanoperedens-like archaea.";
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 -!- 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:KPQ45174.1}.
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DR EMBL; LKCM01000019; KPQ45174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P8E3P3; -.
DR PATRIC; fig|1719120.3.peg.283; -.
DR Proteomes; UP000050360; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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 PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF8; CYSTEINE DESULFURASE-RELATED; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 23..397
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 410 AA; 45407 MW; 436CF30F1BBDEF40 CRC64;
MDIQKIRRDF PALGKKWNGK YPVYLDNACM TLKPEPVIDA MNEYYTEYPV CGGRSIHKMA
KKVDEKVTLS REKFQKFLGA SCPEEIIFTR NTTEGLNLVA NSLDFKNGDI VLTTDREHNS
NLVPWQVQAH KRGVKHIIVY SNPDNTFDLD AFSGLFDKNK NVRLVSMAHT ANLDGYTIPV
KEIIKIAHDN GALMMLDGAQ SAPHKHVDVK ALDVDFFALS VHKMVGPTGM GVLYGKHHLL
EEIAPFIVGG DTVSDTTYES AKFLPTPEKF EAGLQNYAGI IGSGAAVDYI SGVGLSNIEE
HEKRLNTIIT KGIKDMPGLK IIGPEDPNLR GGIISFTVEL PKGGDAHDIA LILDETENIE
VRSGAFCVHS WFNYRKCEAA VRASLYLYNT EDEAKKFVDT LGKTIGLFSP
//
