ID C0M8U3_STRE4 Unreviewed; 380 AA.
AC C0M8U3;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Putative cysteine desulfhydrase {ECO:0000313|EMBL:CAW93571.1};
GN OrderedLocusNames=SEQ_0996 {ECO:0000313|EMBL:CAW93571.1};
OS Streptococcus equi subsp. equi (strain 4047).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553482 {ECO:0000313|EMBL:CAW93571.1, ECO:0000313|Proteomes:UP000001365};
RN [1] {ECO:0000313|EMBL:CAW93571.1, ECO:0000313|Proteomes:UP000001365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4047 {ECO:0000313|EMBL:CAW93571.1,
RC ECO:0000313|Proteomes:UP000001365};
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
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. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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DR EMBL; FM204883; CAW93571.1; -; Genomic_DNA.
DR RefSeq; WP_012679445.1; NC_012471.1.
DR AlphaFoldDB; C0M8U3; -.
DR KEGG; seu:SEQ_0996; -.
DR HOGENOM; CLU_003433_0_0_9; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000001365; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.260.50; -; 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; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11601:SF50; CYSTEINE DESULFURASE ISCS 2-RELATED; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 2..365
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 380 AA; 41570 MW; 2BDE05B71E1BAB75 CRC64;
MIYFDNAATT KPYEEALKTY QEVASKIYGN PSSLHQLGAN ASRILEASRR QIAALLDVEA
KEIFFTSGGT ESDNWAIKGI AFEKSHFGKH IIVSAIEHPA VRESAKWLES QGFELSYAPV
TDKGVVDVKK LAALIRKDTI LVSIMAVNNE IGSIQPIAAI SELLADKPTI TFHVDAVQAI
GKLPVEAYLT ARVDLASFSG HKFHAVRGVG FLYKKSGKRI TPLLVGGGQE DELRSTTENV
AAIASMAKAL RIITERQDRS QARIAAMKKV IYQALQAYED TILFSEIDDF APHILTFGIK
GVRGEVIVHA FEKHEIYIST TSACSSKVGK PAGTLVSMGI PAALAQTAVR ISLDDDNDMG
QVEQFLTIFK QIYEKTQKVR
//
