ID   A0A0A0IZR4_9MICO        Unreviewed;       130 AA.
AC   A0A0A0IZR4;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Cystathionine beta-lyase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=N801_06710 {ECO:0000313|EMBL:KGN29954.1};
OS   Knoellia aerolata DSM 18566.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Knoellia.
OX   NCBI_TaxID=1385519 {ECO:0000313|EMBL:KGN29954.1, ECO:0000313|Proteomes:UP000030013};
RN   [1] {ECO:0000313|EMBL:KGN29954.1, ECO:0000313|Proteomes:UP000030013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18566 {ECO:0000313|EMBL:KGN29954.1,
RC   ECO:0000313|Proteomes:UP000030013};
RA   Zhu W., Wang G.;
RT   "The genome sequence of Knoellia aerolata.";
RL   Submitted (AUG-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGN29954.1}.
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DR   EMBL; AVPL01000192; KGN29954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0IZR4; -.
DR   eggNOG; COG0626; Bacteria.
DR   Proteomes; UP000030013; 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; 3.40.640.10; 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   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   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:UP000030013}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGN29954.1"
FT   NON_TER         130
FT                   /evidence="ECO:0000313|EMBL:KGN29954.1"
SQ   SEQUENCE   130 AA;  13868 MW;  8A8026B7ED741901 CRC64;
     CYGALKTFGE KWLAHMGVDV ELYDPSIGAG IEALIRPATR MICIEAPGTV TMEMADVPAI
     AAAARRHGVL TMMDNTWASP LGFQPLAHGV DFSVEAATKF FGGHSDVLMG SISMNDAGHY
     AVLRETQSIL
//