ID   A1SSS1_PSYIN            Unreviewed;       407 AA.
AC   A1SSS1;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   04-NOV-2026, entry version 100.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ABM02536.1};
DE            EC=4.4.1.8 {ECO:0000313|EMBL:ABM02536.1};
GN   OrderedLocusNames=Ping_0683 {ECO:0000313|EMBL:ABM02536.1};
OS   Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM02536.1, ECO:0000313|Proteomes:UP000000639};
RN   [1] {ECO:0000313|EMBL:ABM02536.1, ECO:0000313|Proteomes:UP000000639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37 {ECO:0000313|EMBL:ABM02536.1,
RC   ECO:0000313|Proteomes:UP000000639};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L,L-cystathionine + H2O = L-homocysteine + pyruvate + NH4(+);
CC         Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC         Evidence={ECO:0000256|ARBA:ARBA00047517};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-substituted L-cysteine + H2O = a thiol + pyruvate +
CC         NH4(+); Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00047625};
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-methionine biosynthesis via de novo
CC       pathway; L-homocysteine from L-cystathionine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00046315}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000510; ABM02536.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1SSS1; -.
DR   STRING; 357804.Ping_0683; -.
DR   KEGG; pin:Ping_0683; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_5_1_6; -.
DR   OMA; AALMIFQ; -.
DR   Proteomes; UP000000639; Chromosome.
DR   GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; 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   FunFam; 3.40.640.10:FF:000046; Cystathionine gamma-lyase; 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; IPR006233; Cys_b_lyase_bac.
DR   InterPro; IPR054542; Cys_met_metab_PP.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01324; cysta_beta_ly_B; 1.
DR   NCBIfam; NF006538; PRK09028.1; 1.
DR   PANTHER; PTHR43500; CYSTATHIONINE BETA-LYASE-RELATED; 1.
DR   PANTHER; PTHR43500:SF1; CYSTATHIONINE BETA-LYASE-RELATED; 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:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ABM02536.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000639}.
FT   MOD_RES         220
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   407 AA;  45362 MW;  473F920D31F945B7 CRC64;
     MLIWYYLRYL PMEINMKKET QIVCLGRNKK WTKGVVNPPV VRASTMLFDT MEDMRFAGKN
     KNNGEMYYGR RGGPTHFAFQ EAIAELEGGA GTALYPSGTA AISSALMSFL KAGDHLLMLD
     NAYEPTRALC DTLLAGFGIE TTYYDPLIGA GISELIQPNT KVLFLESPGS ITMEIQDVPT
     LSRIAHENNL IVMLDNTWAS PINSRPFEMG VDISIQAATK YIVGHSDVMM GTATANTKYW
     PTLREHSYLL GQCTSPDDVY LASRGLRTLG VRMAQHEKNA LAVANWLATR PEVDHLRHPA
     FETCPGHEFF KRDFSGSNGL FSFVLKEGNL KSVTALVENM DYFKMGFSWG GFESLILGVF
     GIDKIRTVTQ WDKSKPLIRL HVGLENVDDL IADLEAGFER MNKALSK
//