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Database: UniProt
Entry: A0A1R4ABE2_BABMR
LinkDB: A0A1R4ABE2_BABMR
Original site: A0A1R4ABE2_BABMR 
ID   A0A1R4ABE2_BABMR        Unreviewed;       415 AA.
AC   A0A1R4ABE2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   ORFNames=BMR1_03g01415 {ECO:0000313|EMBL:SJK86341.1};
OS   Babesia microti (strain RI).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=1133968 {ECO:0000313|EMBL:SJK86341.1, ECO:0000313|Proteomes:UP000002899};
RN   [1] {ECO:0000313|EMBL:SJK86341.1, ECO:0000313|Proteomes:UP000002899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RI {ECO:0000313|EMBL:SJK86341.1,
RC   ECO:0000313|Proteomes:UP000002899};
RX   PubMed=22833609; DOI=10.1093/nar/gks700;
RA   Cornillot E., Hadj-Kaddour K., Dassouli A., Noel B., Ranwez V.,
RA   Vacherie B., Augagneur Y., Bres V., Duclos A., Randazzo S., Carcy B.,
RA   Debierre-Grockiego F., Delbecq S., Moubri-Menage K., Shams-Eldin H.,
RA   Usmani-Brown S., Bringaud F., Wincker P., Vivares C.P., Schwarz R.T.,
RA   Schetters T.P., Krause P.J., Gorenflot A., Berry V., Barbe V.,
RA   Ben Mamoun C.;
RT   "Sequencing of the smallest Apicomplexan genome from the human pathogen
RT   Babesia microti.";
RL   Nucleic Acids Res. 40:9102-9114(2012).
RN   [2] {ECO:0000313|EMBL:SJK86341.1, ECO:0000313|Proteomes:UP000002899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RI {ECO:0000313|EMBL:SJK86341.1,
RC   ECO:0000313|Proteomes:UP000002899};
RX   PubMed=27752055; DOI=10.1038/srep35284;
RA   Silva J.C., Cornillot E., McCracken C., Usmani-Brown S., Dwivedi A.,
RA   Ifeonu O.O., Crabtree J., Gotia H.T., Virji A.Z., Reynes C., Colinge J.,
RA   Kumar V., Lawres L., Pazzi J.E., Pablo J.V., Hung C., Brancato J.,
RA   Kumari P., Orvis J., Tretina K., Chibucos M., Ott S., Sadzewicz L.,
RA   Sengamalay N., Shetty A.C., Su Q., Tallon L., Fraser C.M., Frutos R.,
RA   Molina D.M., Krause P.J., Ben Mamoun C.;
RT   "Genome-wide diversity and gene expression profiling of Babesia microti
RT   isolates identify polymorphic genes that mediate host-pathogen
RT   interactions.";
RL   Sci. Rep. 6:35284-35284(2016).
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; LN871598; SJK86341.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4ABE2; -.
DR   VEuPathDB; PiroplasmaDB:BMR1_03g01415; -.
DR   OrthoDB; 227788at2759; -.
DR   Proteomes; UP000002899; Chromosome IIIa.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
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; PTHR43586; CYSTEINE DESULFURASE; 1.
DR   PANTHER; PTHR43586:SF8; CYSTEINE DESULFURASE-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000002899};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:SJK86341.1}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..415
FT                   /note="cysteine desulfurase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010294518"
FT   DOMAIN          45..402
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   415 AA;  45832 MW;  4F2330B19862FD76 CRC64;
     MHSSTALFNP LYLLITISQA LCFNNEIRSQ FPILNRPVTD KQRLVYLDNA AGAQVPAQTI
     NVIKDYYELY NSNVFKSQHF IAQQTTQLYK QALDDIAMFI GAKADNLIIT SGATQAIQIA
     ASSISHNFNE GDEIILSNLE HSSNVIPWKI LALKQKLNIK YAKIDKNGHV DVDKLLKLIT
     GRTKLISLVY ASSVLGTLLD TERIASICQQ KKILFMLDGC QASPHLLIDV GILGCDLFVS
     SGHKIYGPTG VGFLYASTNI FGKLIYPFNQ YQTSGVSPFS LVDFQGTPPI AQVLGLASSL
     NFLKQNLPQI IPYEAELREY LVEQLLMVPG LDVYMHDGKV PIVSFNIKNT SPIDISIYLD
     TLGIAIRAGQ HCSPLSHNYL NVPATCRVSL AMYNDKSDID RLVSGLKQFV SITAV
//
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