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Database: UniProt
Entry: S9VP05_9TRYP
LinkDB: S9VP05_9TRYP
Original site: S9VP05_9TRYP 
ID   S9VP05_9TRYP            Unreviewed;       474 AA.
AC   S9VP05;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:EPY25040.1};
GN   ORFNames=STCU_04120 {ECO:0000313|EMBL:EPY30330.1}, STCU_06873
GN   {ECO:0000313|EMBL:EPY25040.1};
OS   Strigomonas culicis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX   NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY25040.1, ECO:0000313|Proteomes:UP000015354};
RN   [1] {ECO:0000313|EMBL:EPY25040.1, 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   [2] {ECO:0000313|EMBL:EPY25040.1}
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPY25040.1}.
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DR   EMBL; ATMH01006873; EPY25040.1; -; Genomic_DNA.
DR   EMBL; ATMH01004120; EPY30330.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9VP05; -.
DR   EnsemblProtists; EPY25040; EPY25040; STCU_06873.
DR   EnsemblProtists; EPY30330; EPY30330; STCU_04120.
DR   OrthoDB; 6018at2759; -.
DR   Proteomes; UP000015354; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; 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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808:SF15; CYSTATHIONINE GAMMA-LYASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015354};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   MOD_RES         286
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   474 AA;  52516 MW;  928B5BCE4F4073E0 CRC64;
     MYTYVNRYRL THLFTYLSLP LSLVLLVWYF FFNFKESYQL VFTSSFLFVC FPALFFSLPS
     PIPAFNMSAH QHLVSDATVG SGAWLPEAQG FDTLQVHGGV RPDPVTGAIL TPLYQSTTFV
     QESIDKYQQR GYSYTRSANP TVKVLEERLC ALENGAYATA YSTGMAATTT AISAYMSQGD
     HAIVTDCSYG GTNRACRLFF TRMGMEFTFV DMRDVKNVEA AIKPNTKLVI SESPANPTLT
     LIDIQALSTL CRAKNIIHMC DNTFATALIM RPLDHDCDVT LISTTKYVDG HDMTVGGALV
     TKSKELDDKV RYVQNILGNA MSPYVAYLQL QTSKTMSLRV TKQSESAQKI AEFLEKHSAV
     ETVHYPGLAS FPQKALADRQ HRNHLHGGML WFEVKGGTAA GRKLMDTVPR PWSLCENLGA
     CESIITCPSV MTHANMTTED RLKVGITDGF VRVSVGVEDA EDLIRALKVA LDAL
//
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