ID A0A0F2E1J6_STROR Unreviewed; 408 AA.
AC A0A0F2E1J6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=csdB {ECO:0000313|EMBL:KJQ77158.1};
GN ORFNames=TZ95_01006 {ECO:0000313|EMBL:KJQ77158.1};
OS Streptococcus oralis subsp. tigurinus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1077464 {ECO:0000313|EMBL:KJQ77158.1, ECO:0000313|Proteomes:UP000033377};
RN [1] {ECO:0000313|EMBL:KJQ77158.1, ECO:0000313|Proteomes:UP000033377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC5873 {ECO:0000313|EMBL:KJQ77158.1,
RC ECO:0000313|Proteomes:UP000033377};
RA Haase E.M.;
RT "Evolution of amylase-binding proteins of oral streptococcal species.";
RL Submitted (FEB-2015) 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}.
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:KJQ77158.1}.
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DR EMBL; JYGU01000006; KJQ77158.1; -; Genomic_DNA.
DR RefSeq; WP_045617307.1; NZ_JYGU01000006.1.
DR AlphaFoldDB; A0A0F2E1J6; -.
DR PATRIC; fig|28037.217.peg.981; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000033377; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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 Lyase {ECO:0000313|EMBL:KJQ77158.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004506};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 24..393
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 408 AA; 45156 MW; 9086DA900C3EA8ED CRC64;
MLDVEAIRKD FPILDQIVND EPLVYLDNAA TTQKPLAVLE TITRYYEQDN ANVHRGVHTL
AERATASYEA ARETIRKFIN ASSTKEVLFT RGTTTSLNWV ARFAEEILTE GDQVLISVME
HHSNIIPWQE ACRKTGAELV YAYLKDGSLD MADLQVKLTD KVKFVSLAHA SNVLGVVNPI
KEITQMAHQV GAIMVVDGAQ STPHMKIDVQ DLDVDFFAFS GHKMAGPTGI GVLYGKEKYL
NQMSPVEFGG EMIDFVYEQS ASWKELPWKF EAGTPNMAGA IGLAAAVDYL EKIGMDAIEA
HEQELIAYVY PKLQAIEGLT IYGSQDLAQR SGVIAFNLGE LHPHDLATAL DYEGVAVRAG
HHCAQPLLQY LDVPATARAS FYIYNTKADC DKLVDALQKT KEFFNGTF
//
