ID A0A0D2KZM1_9CHLO Unreviewed; 506 AA.
AC A0A0D2KZM1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Cystathionine gamma-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MNEG_7345 {ECO:0000313|EMBL:KIZ00619.1};
OS Monoraphidium neglectum.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ00619.1, ECO:0000313|Proteomes:UP000054498};
RN [1] {ECO:0000313|EMBL:KIZ00619.1, ECO:0000313|Proteomes:UP000054498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ00619.1,
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; KK101509; KIZ00619.1; -; Genomic_DNA.
DR RefSeq; XP_013899638.1; XM_014044184.1.
DR AlphaFoldDB; A0A0D2KZM1; -.
DR STRING; 145388.A0A0D2KZM1; -.
DR GeneID; 25740221; -.
DR KEGG; mng:MNEG_7345; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000054498; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
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); 2.
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; 3.
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|RuleBase:RU362118};
KW Reference proteome {ECO:0000313|Proteomes:UP000054498}.
SQ SEQUENCE 506 AA; 52144 MW; 83EF1D262B5F653E CRC64;
MAAQPANGQH EAQASAAAPT SGAHAGSYEF ATEAIHGGQR VCPVTGAVFP PLYTSSTFAQ
QSPGVHQGYE YSRSHNPTRF AFERSYAVLE GTGLTEEQDT TRGAFAFASG LAAGACVLEL
LDAGSTVVCI DDVYGGTFRL LNRVRARTAS LKIVRADLAD DVAAEAAIVG AASNGSGAAD
SNGGAGVGSK VGLVWLETPT NPTLKLADIA KVAELAHKAG ALLVVDNTFA TPALTRPLQL
GADIVLSSTT KYVAGHSDTG CGQRRTCGGR TRVGLRRALG AASRGTACGA WRVPPPAVGG
VLATRHADVA ERLRFLQNAV GSVMSPWDAY LTLRGAKTLH VRIQRHCENA LELARRLEGA
AAVARVVYPG LESHPQHALA ARQMRLPDAG PGRRGADAAA FGGMISLTLK GGLAESRAFL
EALRVFTLAE SLGGVESLAE HPALMTHGSV PADERAKLGI DDGFVRLSVG IEHVEDLWAD
LEGALAAAAA AGKRAGAAAA AAREES
//
