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Database: UniProt
Entry: F9UT53_LACPL
LinkDB: F9UT53_LACPL
Original site: F9UT53_LACPL 
ID   F9UT53_LACPL            Unreviewed;       381 AA.
AC   F9UT53;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Cystathionine beta-lyase / cystathionine gamma-lyase {ECO:0000313|EMBL:CCC77784.1};
DE            EC=4.4.1.1 {ECO:0000313|EMBL:CCC77784.1};
DE            EC=4.4.1.8 {ECO:0000313|EMBL:CCC77784.1};
GN   Name=cblB {ECO:0000313|EMBL:CCC77784.1};
GN   OrderedLocusNames=lp_0255 {ECO:0000313|EMBL:CCC77784.1};
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668 {ECO:0000313|EMBL:CCC77784.1, ECO:0000313|Proteomes:UP000000432};
RN   [1] {ECO:0000313|EMBL:CCC77784.1, ECO:0000313|Proteomes:UP000000432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC   {ECO:0000313|Proteomes:UP000000432};
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W., Stiekema W.,
RA   Lankhorst R.M., Bron P.A., Hoffer S.M., Groot M.N., Kerkhoven R.,
RA   de Vries M., Ursing B., de Vos W.M., Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WCFS1;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.F.T.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CCC77784.1, ECO:0000313|Proteomes:UP000000432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC   {ECO:0000313|Proteomes:UP000000432};
RX   PubMed=22156394; DOI=10.1128/JB.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.F.T.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
RN   [4] {ECO:0007829|PDB:6LDO, ECO:0007829|PDB:6LE4}
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
RX   PubMed=32913258; DOI=10.1038/s41598-020-71756-7;
RA   Matoba Y., Noda M., Yoshida T., Oda K., Ezumi Y., Yasutake C.,
RA   Izuhara-Kihara H., Danshiitsoodol N., Kumagai T., Sugiyama M.;
RT   "Catalytic specificity of the Lactobacillus plantarum cystathionine gamma-
RT   lyase presumed by the crystallographic analysis.";
RL   Sci. Rep. 10:14886-14886(2020).
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|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; AL935263; CCC77784.1; -; Genomic_DNA.
DR   RefSeq; WP_011100941.1; NC_004567.2.
DR   RefSeq; YP_004888298.1; NC_004567.2.
DR   PDB; 6LDO; X-ray; 2.75 A; A/B/C/D/E/F=1-381.
DR   PDB; 6LE4; X-ray; 3.10 A; A/B/C/D/E/F=1-381.
DR   AlphaFoldDB; F9UT53; -.
DR   SMR; F9UT53; -.
DR   STRING; 220668.lp_0255; -.
DR   EnsemblBacteria; CCC77784; CCC77784; lp_0255.
DR   GeneID; 77216908; -.
DR   KEGG; lpl:lp_0255; -.
DR   PATRIC; fig|220668.9.peg.211; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_0_9; -.
DR   OrthoDB; 9780685at2; -.
DR   PhylomeDB; F9UT53; -.
DR   Proteomes; UP000000432; Chromosome.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:UniProtKB-EC.
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: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:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 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.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:6LDO, ECO:0007829|PDB:6LE4};
KW   Lyase {ECO:0000313|EMBL:CCC77784.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000432}.
FT   MOD_RES         194
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   381 AA;  40865 MW;  1E676C0B3FF466F4 CRC64;
     MKFETQLIHG GISEDATTGA TSVPIYMAST FRQTKIGQNQ YEYSRTGNPT RAAVEALIAT
     LEHGSAGFAF ASGSAAINTV FSLFSAGDHI IVGNDVYGGT FRLIDAVLKH FGMTFTAVDT
     RDLAAVEAAI TPTTKAIYLE TPTNPLLHIT DIAAIAKLAQ AHDLLSIIDN TFASPYVQKP
     LDLGVDIVLH SASKYLGGHS DVIGGLVVTK TPALGEKIGY LQNAIGSILA PQESWLLQRG
     MKTLALRMQA HLNNAAKIFT YLKSHPAVTK IYYPGDPDNP DFSIAKQQMN GFGAMISFEL
     QPGMNPQTFV EHLQVITLAE SLGALESLIE IPALMTHGAI PRTIRLQNGI KDELIRLSVG
     VEASDDLLAD LERGFASIQA D
//
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