ID   A0A0K6IAQ7_9BURK        Unreviewed;       410 AA.
AC   A0A0K6IAQ7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Cystathionine beta-lyase, bacterial {ECO:0000313|EMBL:CUB00220.1};
GN   ORFNames=Ga0061069_11229 {ECO:0000313|EMBL:CUB00220.1};
OS   Thiomonas bhubaneswarensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=339866 {ECO:0000313|EMBL:CUB00220.1, ECO:0000313|Proteomes:UP000183649};
RN   [1] {ECO:0000313|Proteomes:UP000183649}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18181 {ECO:0000313|Proteomes:UP000183649};
RA   Varghese N.;
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
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:ARBA00001535};
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; CYHF01000012; CUB00220.1; -; Genomic_DNA.
DR   RefSeq; WP_055451636.1; NZ_LIPV01000012.1.
DR   AlphaFoldDB; A0A0K6IAQ7; -.
DR   STRING; 339866.GCA_001418255_02815; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000183649; Unassembled WGS sequence.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; IPR006233; Cys_b_lyase_bac.
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   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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:CUB00220.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         224
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   410 AA;  44003 MW;  14025D5283A88576 CRC64;
     MSSQQEPQLD QKPLPSSENL ALSTRLQHHP YQAPAGFDAV EPGVHHASTV IFPNVAAMRA
     RDWRSKAGYT YGLHGTPTTF ILEERLAALD GGRHCVLCPS GLSAIALVDL ALLQQGDTVL
     LPSNVYGPSR ELAECFLGAW GIEHRLYDAS CTPDELAALI TPQTKLLWLE APGSVTMEMP
     DLRGFIGVAR QHGVLTAIDA TWAAGIALKP FDLGVDVVMQ ALTKYQSGGA DVLMGSVTTR
     DDALHERLLL THMRLGLGVS GDDAARVLRG LHTLALRYAA HDASARQIAR WMQQQAAVAQ
     VLHPALPGSP GHAFWQRDCT AAGGLFSVLF QPRYTAAQID AFVDALRLFK IGYSWGGPVS
     LAVPYDVQLM RPSSHWPHAG GLVRLAIGLE DPQDLIDDLA RALGAAGMAG
//