ID A8DW64_NEMVE Unreviewed; 242 AA.
AC A8DW64;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=cystathionine gamma-lyase {ECO:0000256|ARBA:ARBA00012085};
DE EC=4.4.1.1 {ECO:0000256|ARBA:ARBA00012085};
DE AltName: Full=Gamma-cystathionase {ECO:0000256|ARBA:ARBA00029853};
GN ORFNames=NEMVEDRAFT_v1g157094 {ECO:0000313|EMBL:EDO25544.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO25544.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO25544.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-homocysteine and L-serine: step 2/2.
CC {ECO:0000256|ARBA:ARBA00005038}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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DR EMBL; DS479194; EDO25544.1; -; Genomic_DNA.
DR RefSeq; XP_001617644.1; XM_001617594.1.
DR AlphaFoldDB; A8DW64; -.
DR STRING; 45351.A8DW64; -.
DR EnsemblMetazoa; EDO25544; EDO25544; NEMVEDRAFT_v1g157094.
DR KEGG; nve:5495802; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_8_0_1; -.
DR InParanoid; A8DW64; -.
DR OMA; QTHDDVA; -.
DR PhylomeDB; A8DW64; -.
DR UniPathway; UPA00136; UER00202.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-UniPathway.
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:SF90; CYSTATHIONINE GAMMA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362118};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDO25544.1"
SQ SEQUENCE 242 AA; 26365 MW; 7F664DA4849F0224 CRC64;
LYAETPTNPG VDVLDLDLLG NIAKKHNLLL IIDNCFATPY LQKPIDFGAD IVLHSATKLI
DGQGRVLGGV AVGKETLIRE IYLFSRNTGP AMSPFNAWIL SKSLETLVVR VEKHCENALK
VAQFLEGHSK VNLVKHPFLA SHPQYEIAKK QMRLGGNIVA FEVTGGVEAG REFLNAIKLC
SLSANLGDTR TIVTHPASTT HSKLTNEDRL EAGITDGLVR VSVGLEHVED IINDLKQALE
NV
//
