ID I0YVR8_COCSC Unreviewed; 419 AA.
AC I0YVR8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 13-SEP-2023, entry version 46.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:EIE22487.1};
GN ORFNames=COCSUDRAFT_37091 {ECO:0000313|EMBL:EIE22487.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE22487.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE22487.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE22487.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
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:EIE22487.1}.
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DR EMBL; AGSI01000010; EIE22487.1; -; Genomic_DNA.
DR RefSeq; XP_005647031.1; XM_005646974.1.
DR AlphaFoldDB; I0YVR8; -.
DR STRING; 574566.I0YVR8; -.
DR GeneID; 17040473; -.
DR KEGG; csl:COCSUDRAFT_37091; -.
DR eggNOG; KOG0053; Eukaryota.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000007264; 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 PIRSF; PIRSF001434; CGS; 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:EIE22487.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007264}.
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 419 AA; 44608 MW; E4266850D2480A6F CRC64;
MATRLVHAPK VTSDPYGAVS PPLYQTATFE QVSAVECGRY DYSRSGNPTR TQLEAHIAHL
EGAARSFAFG SGMAALSAVL RLVRNGEHVV AGDDIYGGTS RLLTRVAPDL GISVTNVSTT
ETEPLRQAII PGKTKLVMLE SPTNPRMQIC DIAALTAIAH EAGALVVVDN SILAPTFQQP
LVLGADIVMT SATKFIAGHS DVTGGLLSVR DPELAERVYF YQNAEGSGLG PFDCWLAMRG
LKTMALRMER QAASAALIAR WLQAHPLVRK VNYPGLPSHP GHAVHAAQSS SGGSLLSFET
GSIEASRTVA EQAQLFKITV SFGSVSSLIS LPCYMSHASI PAALRVQRGL PDDLVRISVG
IEDPADLLAD LDQAMRKAMD AIGMTAAVPG FQLDGFTGSQ RERQLLDRIA QLEAQLQPT
//
