ID A0A061EW34_THECC Unreviewed; 484 AA.
AC A0A061EW34;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Cystathionine beta-lyase isoform 1 {ECO:0000313|EMBL:EOY09021.1};
GN ORFNames=TCM_024360 {ECO:0000313|EMBL:EOY09021.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY09021.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY09021.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001883; EOY09021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061EW34; -.
DR STRING; 3641.A0A061EW34; -.
DR EnsemblPlants; EOY09021; EOY09021; TCM_024360.
DR Gramene; EOY09021; EOY09021; TCM_024360.
DR eggNOG; KOG0053; Eukaryota.
DR InParanoid; A0A061EW34; -.
DR OMA; IMMANHA; -.
DR Proteomes; UP000026915; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
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:SF50; CYSTATHIONINE BETA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT MOD_RES 280
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 484 AA; 52766 MW; E2DF304FA4D2CF4A CRC64;
MASSLPLRPF LSSIYSVPNH KNGPLLENFP RSSEVNKELY LERRQLLSGK RFRLNCLGHR
DMDVSASVLV ESVTECSAEL NVEHQEPSIS TLLMNIESNF DPYGAMSTPL YQTATFKQPS
AIDNGPYDYT RSGNPTRDVL ERLLAKLEKA DRAFCFTSGM AALSAVAQLV GTGEEIVAGD
DIYGGSDRLL SQVTPKYGVV VKRVNTSDLD EVRAVIGPKT KLVWLESPTN PRQQIADIRR
IAEMAHAYGA LMLVDNSIMS PVLSQPLKLG ADIVMHSATK FIAGHSDVMA GVLAVKGESL
AEQLYFLQNA VGSGLAPFDC WICLRGIKTM ALRIEKQQEN AQKIAEFLSS HSLVKKENAQ
KIAEFLSSHP LVKKVNYAGL PDHPGRDLHY SQAKGAGSVL SFLTGSLALS KHVVETTKYF
SITVSFGSVK SLISMPCFMS HASIPSAVRE ARGLTEDLVR ISVGIEDVND LIADLDNALR
TGPL
//
