ID Q8DQA2_STRR6 Unreviewed; 408 AA.
AC Q8DQA2;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 131.
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 OrderedLocusNames=spr0773 {ECO:0000313|EMBL:AAK99577.1};
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101 {ECO:0000313|EMBL:AAK99577.1, ECO:0000313|Proteomes:UP000000586};
RN [1] {ECO:0000313|EMBL:AAK99577.1, ECO:0000313|Proteomes:UP000000586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6 {ECO:0000313|Proteomes:UP000000586};
RX PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
RA Hoskins J.A., Alborn W.Jr., Arnold J., Blaszczak L., Burgett S.,
RA DeHoff B.S., Estrem S., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A., LaGace R., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S., McHenney M.,
RA McLeaster K., Mundy C., Nicas T.I., Norris F.H., O'Gara M., Peery R.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C., Baltz R.H., Jaskunas S.Richard.,
RA Rosteck P.R.Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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; AE007317; AAK99577.1; -; Genomic_DNA.
DR PIR; E97968; E97968.
DR RefSeq; NP_358367.1; NC_003098.1.
DR RefSeq; WP_000887734.1; NC_003098.1.
DR AlphaFoldDB; Q8DQA2; -.
DR STRING; 171101.spr0773; -.
DR KEGG; spr:spr0773; -.
DR PATRIC; fig|171101.6.peg.856; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_5_9; -.
DR Proteomes; UP000000586; Chromosome.
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; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004506};
KW Reference proteome {ECO:0000313|Proteomes:UP000000586};
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; 45134 MW; 78123754B0EF9D71 CRC64;
MLDVEAIRKD FPILDQIVND EPLVYLDNAA TTQKPLVVLK AINSYYEQDN ANVHRGVHTL
AERATASYEA ARETIRKFIN AGSTKEVLFT RGTTTSLNWV ARFAEEILTE GDQVLISVME
HHSNIIPWQE ACRKTGAELV YVYLKDGALD MEGLRAKLTD KVKFVSLAHA SNVLGVVNPI
KEITQLAHQV GAIMVVDGAQ STPHMKIDVQ DLDLDFFAFS AHKMAGPTGI GVLYGKEKYL
EQMSPVEFGG EMIDFVYEQS ASWKELPWKF EAGTPNMAGA IGLATAVDYL EKIGMDAIEA
HEQELIAYVY PKLQAIEGLT IYGSQDLAQR SGVIAFNLGD LHPHDLATAL DYEGVAVRAG
HHCAQPLLQY LEVPATARAS FYIYNTKADC DKLVDALQKT KEFFNGTF
//
