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Database: UniProt
Entry: E5RDC8_CUCME
LinkDB: E5RDC8_CUCME
Original site: E5RDC8_CUCME 
ID   E5RDC8_CUCME            Unreviewed;       417 AA.
AC   E5RDC8;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:ADN33936.1};
OS   Cucumis melo subsp. melo.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=412675 {ECO:0000313|EMBL:ADN33936.1};
RN   [1] {ECO:0000313|EMBL:ADN33936.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Young leaves {ECO:0000313|EMBL:ADN33936.1};
RX   PubMed=20509895; DOI=10.1186/1471-2164-11-339;
RA   Gonzalez V.M., Garcia-Mas J., Arus P., Puigdomenech P.;
RT   "Generation of a BAC-based physical map of the melon genome.";
RL   BMC Genomics 11:339-339(2010).
RN   [2] {ECO:0000313|EMBL:ADN33936.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Young leaves {ECO:0000313|EMBL:ADN33936.1};
RX   PubMed=21073723; DOI=10.1186/1471-2229-10-246;
RA   Gonzalez V.M., Benjak A., Henaff E.M., Mir G., Casacuberta J.M.,
RA   Garcia-Mas J., Puigdomenech P.;
RT   "Sequencing of 6.7 Mb of the melon genome using a BAC pooling strategy.";
RL   BMC Plant Biol. 10:246-246(2010).
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; HM854776; ADN33936.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5RDC8; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         214
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   417 AA;  45169 MW;  FF4F04878C4BED0A CRC64;
     MISSLLEDPA AAIANTRHEF GEHGGVNMSI EASATFTVME PETMRRMFAG ELGPDRDFFI
     YSRHFNPTVL NLSRQMAALE GTAAAYCTSS GMSAIAAVLL QLLASGDHVV ASRTLYGGTH
     ALMAHFFPRT SNITTTFVDI GDLKEVEKAI VEGKTKVLYF ESVSNPTLAV ANIPELCRIG
     HEKGVTVVVD NTFAPMILSP ARLGADVVVH SISKFISGGA DIIAGAVCGP TKLVNSMMDL
     RQGSLMLLGP TMNAKVAFEL SERIPHLSLR MKEHCRRASV FAERMKKAGL KVIYPGLEDH
     PQHQLMKSLA NPEYGFGGML CVDMGTEERA NKLMSILQNT TQFGFMAVSL GYYETLMSCS
     GSSTSSEMSG EERELAGISP GLVRMSIGYM GTLEQKWSQF EKALAKVQDI GVPFCNN
//
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