ID A0A0D2MAU9_9CHLO Unreviewed; 377 AA.
AC A0A0D2MAU9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 28-JUN-2023, entry version 34.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KIZ00400.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:KIZ00400.1};
GN ORFNames=MNEG_7562 {ECO:0000313|EMBL:KIZ00400.1};
OS Monoraphidium neglectum.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ00400.1, ECO:0000313|Proteomes:UP000054498};
RN [1] {ECO:0000313|EMBL:KIZ00400.1, ECO:0000313|Proteomes:UP000054498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ00400.1,
RC ECO:0000313|Proteomes:UP000054498};
RX PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA Mussgnug J.H., Kruse O.;
RT "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT neglectum from its genome sequence reveals characteristics suitable for
RT biofuel production.";
RL BMC Genomics 14:926-926(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; KK101567; KIZ00400.1; -; Genomic_DNA.
DR RefSeq; XP_013899419.1; XM_014043965.1.
DR AlphaFoldDB; A0A0D2MAU9; -.
DR STRING; 145388.A0A0D2MAU9; -.
DR GeneID; 25740438; -.
DR KEGG; mng:MNEG_7562; -.
DR OrthoDB; 297744at2759; -.
DR Proteomes; UP000054498; Unassembled WGS sequence.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
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; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000054498};
KW Transferase {ECO:0000313|EMBL:KIZ00400.1}.
FT MOD_RES 186
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 377 AA; 39422 MW; CA876D8E8DEE5B95 CRC64;
MRFQAAEPMS DLLPPTLQFE GTEEGYDNVR YTRCNNNPSQ TAVAAHLAAL EGTEAALPVA
SGMAAISSTL LALLEPGAHI LIVRGPYGGT HDLVASLLKK WGVTSSAVSP EDGPEQWEAL
LQPGKTRLFY AEAISNPLCE VYDLAGIAKF AREHKLLSVI DATFASPVNL QPAKLGFDIT
LHSATKYLNG HSDLIAGVVL GGQELIETIR VTANVLGPAI DPHSCFLLSR GLRTLGLRVE
QQNRNALALA QFLSEAGPKV AAVHYPGLKS SKHHKRAAEL FTNGGCGGVF SFELAGGVDA
AEAFLKRLQL PLVAPSLGGV ESLVTRPATT SHAGLTAKER AAAGISDGLI RVAVGVEATG
DLLDDFSQAL AAVPGAA
//
