ID A0A239SZQ6_9STRE Unreviewed; 411 AA.
AC A0A239SZQ6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=csd {ECO:0000313|EMBL:SNU90722.1};
GN ORFNames=SAMEA4412692_01966 {ECO:0000313|EMBL:SNU90722.1};
OS Streptococcus merionis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=400065 {ECO:0000313|EMBL:SNU90722.1, ECO:0000313|Proteomes:UP000215185};
RN [1] {ECO:0000313|EMBL:SNU90722.1, ECO:0000313|Proteomes:UP000215185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13788 {ECO:0000313|EMBL:SNU90722.1,
RC ECO:0000313|Proteomes:UP000215185};
RG Pathogen Informatics;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; LT906439; SNU90722.1; -; Genomic_DNA.
DR RefSeq; WP_018373628.1; NZ_LT906439.1.
DR AlphaFoldDB; A0A239SZQ6; -.
DR STRING; 1123308.GCA_000380085_01056; -.
DR KEGG; smen:SAMEA4412692_1966; -.
DR eggNOG; COG0520; Bacteria.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000215185; Chromosome 1.
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:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR016454; Cysteine_dSase.
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 PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:SNU90722.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004506};
KW Reference proteome {ECO:0000313|Proteomes:UP000215185};
KW Transferase {ECO:0000256|RuleBase:RU004506, ECO:0000313|EMBL:SNU90722.1}.
FT DOMAIN 25..395
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 411 AA; 45200 MW; 4ED88E8846779517 CRC64;
MPFDPQAIRH DFPILDQLVN DEPLVYLDNG ATTQKPQAVL DELLRYYQTD NANVHRGVHT
LAERATQSYE AAREKVRAFI QAKSTKEVLF TRGTTTSLNW VAQHARTFLQ PDDEVLISIM
EHHANLIPWQ QACQATGAKL RYVYLTADGQ LDVADFKTKL TAKTKIISLT HVSNVLGSIN
PIKEITALAH EVGALMVLDA AQSIPHMPID VQELDVDFMA FSGHKMYGPT GIGILYGKAA
LLDEMDPVEF GGEMIDFVSR QEASWKELPW KFEAGTPNMA AAIGLGAGID YLTQLGVNQI
AAHEQALMAY TLPKLAAVEG VTIYGPQNPA ERAGVIAFNL DGLHPHDVAT ALDYEGVAVR
AGHHCAQPLL QYLDIPSTVR ASFGLYNTVA DCDKFIEAIL KTKEYFHGST F
//
