ID A0A0G1U4D5_9BACT Unreviewed; 407 AA.
AC A0A0G1U4D5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
GN ORFNames=UY18_C0007G0017 {ECO:0000313|EMBL:KKU88919.1};
OS Microgenomates group bacterium GW2011_GWF2_47_9.
OC Bacteria.
OX NCBI_TaxID=1618541 {ECO:0000313|EMBL:KKU88919.1, ECO:0000313|Proteomes:UP000034647};
RN [1] {ECO:0000313|EMBL:KKU88919.1, ECO:0000313|Proteomes:UP000034647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms
CC from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to
CC produce L-alanine. {ECO:0000256|RuleBase:RU004506}.
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 ECO:0000256|RuleBase:RU004506};
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. {ECO:0000256|ARBA:ARBA00010447,
CC ECO:0000256|RuleBase:RU004506}.
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:KKU88919.1}.
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DR EMBL; LCPA01000007; KKU88919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1U4D5; -.
DR STRING; 1618541.UY18_C0007G0017; -.
DR PATRIC; fig|1618541.3.peg.220; -.
DR Proteomes; UP000034647; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:UniProtKB-UniRule.
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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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 NCBIfam; TIGR01979; sufS; 1.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004506};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 24..394
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 407 AA; 44468 MW; 0411C6288C4F4D95 CRC64;
MFDPKQVRKD FPILGRVIHD KPLVYLDSGA TSQKPKVVLD AEREYYEQHN ANVHRGAHTL
GDEATQMYQD ARSVVARFIG GQSQEVVFVR NATEALNLVA YAWGLDSLRA GDVILTTEME
HHANLVPWQE VARRTGAKVE LVKVSAQGLL DQEDYKRKLK LKPKLVAIVQ VSNALGTINP
VFEMTRMAHK AGAVVVVDGA QAIPHMSVNV NDLECDFYVF SGHKMLGPMG IGVLWGRGNI
LESMSPFLTG GGMINEVYAD HSTWAQVPEK FEAGTPNVAG AVGIKAAIEY LEGLGMDNIR
KHDEDIVGYA LAKLGEVEQI TLLGGRDASK RSGSVNFIYE GVHAHDVATI LDSLGVAVRS
GHHCTMVLHN ALGITASIRA SFNVYTIHED IERLVVALGK VKQVFGR
//
