ID S9VI47_9TRYP Unreviewed; 514 AA.
AC S9VI47;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 13-SEP-2023, entry version 37.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:EPY26761.1};
DE SubName: Full=Cystathionine betalyase {ECO:0000313|EMBL:AGT02420.1};
GN ORFNames=STCU_06092 {ECO:0000313|EMBL:EPY26761.1};
OS Strigomonas culicis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY26761.1, ECO:0000313|Proteomes:UP000015354};
RN [1] {ECO:0000313|EMBL:AGT02420.1}
RP NUCLEOTIDE SEQUENCE.
RA Alves J.M.P., Klein C., Maia da Silva F., Costa Martins A.G., Serrano M.G.,
RA Buck G.A., Vasconcelos A.T.R., France-Sagot M., Teixeira M.M.G.,
RA Motta M.C.M., Camargo E.P.;
RT "Genomic Cooperation Between Trypanosomatids and Their Bacterial
RT Endosymbionts in the Synthesis of Essential Amino Acids Heavily Influenced
RT by Multiple Lateral Gene Transfer Events.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EPY26761.1, ECO:0000313|Proteomes:UP000015354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23560078;
RA Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M.,
RA Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M.,
RA Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F.,
RA Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K.,
RA Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C.,
RA Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA de Souza W., Schenkman S., de Vasconcelos A.T.;
RT "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their
RT Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae
RT Family.";
RL PLoS ONE 8:E60209-E60209(2013).
RN [3] {ECO:0000313|EMBL:EPY26761.1}
RP NUCLEOTIDE SEQUENCE.
RA Motta M.C.M., Martins A.C.A., Preta C.M.C.C., Silva R., de Souza S.S.,
RA Klein C.C., de Almeida L.G.P., Cunha O.L., Colabardini A.C., Lima B.A.,
RA Machado C.R., Soares C.M.A., de Menezes C.B.A., Bartolomeu D.C.,
RA Grisard E.C., Fantinatti-Garboggini F., Rodrigues-Luiz G.F., Wagner G.,
RA Goldman G.H., Fietto J.L.R., Ciapina L.P., Brocchi M., Elias M.C.,
RA Goldman M.H.S., Sagot M.-F., Pereira M., Stoco P.H., Teixeira S.M.R.,
RA de Mendonca-Neto R.P., Maciel T.E.F., Mendes T.A.O., Urmenyi T.P.,
RA Teixeira M.M.G., de Camargo E.F.P., de Sousa W., Schenkman S.,
RA de Vasconcelos A.T.R.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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DR EMBL; KC140172; AGT02420.1; -; Genomic_DNA.
DR EMBL; ATMH01006092; EPY26761.1; -; Genomic_DNA.
DR AlphaFoldDB; S9VI47; -.
DR EnsemblProtists; EPY26761; EPY26761; STCU_06092.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000015354; Unassembled WGS sequence.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR006238; Cys_b_lyase_euk.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01329; cysta_beta_ly_E; 1.
DR PANTHER; PTHR11808:SF50; CYSTATHIONINE BETA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EPY26761.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362118};
KW Reference proteome {ECO:0000313|Proteomes:UP000015354}.
SQ SEQUENCE 514 AA; 56994 MW; F8E03759388411EC CRC64;
MSVNQKTSDG LQGQLEKDMT AKERIASLET ENLFLREKVA QMEMLHAISV ARNPQHTVLS
ALDEERHKFE EAIQPHNYGN SRTEDYNELP TYPSRPHFSK ATEHPSTQVV IFDGCPTDPY
HPSSTPIYQT ATFVQPDITQ FGPYDYSRSG NPTRTALETL MAKLEGAHSA FAFSSGMAAL
QTLVTVLRSG DALLASSDLY GGMHRLMTQI TAHLNIEIIF VETWNLDKVR EAFRAHANIK
LLHMESPTNP LMRIVDVATI CEIAHAHGSE VSIDNTMMTP IRCTPLTLGC DYVMHSATKF
ISGHSDTMAG VLCTRSPAQS KRIAFLQNAQ GNALAPFDCW LLQRGIKTLA LRVEKQELNA
VAVALFLARQ RHIIKRVHYA GLNPKVFPNM ISSDENSFLL HRRQTSGPGS VMSFETGSVE
RSHRFVRACK LFKLTVSFGS CNSLIEMPCL LSHASIPKEK RTLPDDLIRL SVGIEQIEDI
LADLTKAVEA AEDSDSVTSA SASELTDRDI SRVI
//
