ID A0A061D2E3_BABBI Unreviewed; 826 AA.
AC A0A061D2E3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=BBBOND_0110650 {ECO:0000313|EMBL:CDR94768.1};
OS Babesia bigemina.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR94768.1, ECO:0000313|Proteomes:UP000033188};
RN [1] {ECO:0000313|Proteomes:UP000033188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RX PubMed=24799432; DOI=10.1093/nar/gku322;
RA Jackson A.P., Otto T.D., Darby A., Ramaprasad A., Xia D., Echaide I.E.,
RA Farber M., Gahlot S., Gamble J., Gupta D., Gupta Y., Jackson L.,
RA Malandrin L., Malas T.B., Moussa E., Nair M., Reid AJ., Sanders M.,
RA Sharma J., Tracey A., Quail M.A., Weir W., Wastling J.M., Hall N.,
RA Willadsen P., Lingelbach K., Shiels B., Tait A., Berriman M., Allred D.R.,
RA Pain A.;
RT "The evolutionary dynamics of variant antigen genes in Babesia reveal a
RT history of genomic innovation underlying host-parasite interaction.";
RL Nucleic Acids Res. 42:7113-7131(2014).
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 -!- 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.
CC {ECO:0000256|ARBA:ARBA00010447}.
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DR EMBL; LK391707; CDR94768.1; -; Genomic_DNA.
DR RefSeq; XP_012766954.1; XM_012911500.1.
DR AlphaFoldDB; A0A061D2E3; -.
DR STRING; 5866.A0A061D2E3; -.
DR EnsemblProtists; CDR94768; CDR94768; BBBOND_0110650.
DR GeneID; 24563309; -.
DR KEGG; bbig:BBBOND_0110650; -.
DR VEuPathDB; PiroplasmaDB:BBBOND_0110650; -.
DR OrthoDB; 227788at2759; -.
DR Proteomes; UP000033188; Chromosome 1.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000033188};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..826
FT /note="cysteine desulfurase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001595697"
FT DOMAIN 76..457
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 826 AA; 91659 MW; DB8139D91D1D0F91 CRC64;
MYTRGYIVCL VAFHIFSGAL CLSPTGRLRT SFLHPPTRYN TLHGGRWRLK SDGAERDSPY
VYEFPALNRP ESRNLVYFDN AATTQKPRAV IEAILDYYSN PCANVHRSQH DLATSASTRY
ESARHNVSSF INASSPSEIV FTSGATESIN IVAGSWWWVE KLHVPHRDNV GPGDVILLPL
SEHNSNIIPW QLHANDSGCR IGFIKLTEDG SVDLDDYNRL LDQGNVKLVS LAHASNVIGR
VQDLSTIVRL AHSRGAKVLV DACQTLGHIP IDVSSIGCDF LVGSAHKMYG PTGVGFLYAK
RSILDSMRPH RGGGGMVKNV TTTRFELEDV PHRFESGTPQ VAQVIGFSAA IDFLRDIGLS
KIAAYERELL SYLRDQLCKV ATVYSPALDP NSDEHCPIVS FNVDGVSAFD IAALLATHNI
AVRAGQHCAH ILHRDYLKVD HSLRVSLALY NTRGEIDDRR PFTHGVCTMT LTRSLARLKS
RSPYLGFFRN TPFYRRSGGD SILRVNPRLV PSKQLGKTLL RIGTLGMDRA KLERILITCA
TQMGQALDDV NLSTCLSLMV RLQISNPQCL ESLVPYCYRI SDLERAIACC HLIGMVPGSR
DSPSARAFVV HVSQRVPLEG HSLLLRDLGR LCESLRVLDL YCEDLGEFLA SVIEDELIHS
ESSEDAVYIT SVLGYLGRMG VGSVPLWRLF SRYTATEGIH SNPRVLIKAL ESFCDRRIKH
ESLLNQAGDA LALVLDSLRP SEVARVADVY SRLGFYHKRL AEVLILGAER VTPFLDASDS
VKLLRTFVQA YSQPGTHAAI TQDPSLSHRH RRALYLTFNR CTTGLK
//
