ID   A0A1G9Y5S5_9BACL        Unreviewed;       402 AA.
AC   A0A1G9Y5S5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Cystathionine beta-lyase/cystathionine gamma-synthase {ECO:0000313|EMBL:SDN04482.1};
GN   ORFNames=SAMN04487897_101894 {ECO:0000313|EMBL:SDN04482.1};
OS   Paenibacillus sp. yr247.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1761880 {ECO:0000313|EMBL:SDN04482.1, ECO:0000313|Proteomes:UP000198936};
RN   [1] {ECO:0000313|EMBL:SDN04482.1, ECO:0000313|Proteomes:UP000198936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR247 {ECO:0000313|EMBL:SDN04482.1,
RC   ECO:0000313|Proteomes:UP000198936};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU362118}.
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DR   EMBL; FNIF01000001; SDN04482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9Y5S5; -.
DR   STRING; 1761880.SAMN04487897_101894; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000198936; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:SDN04482.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198936}.
FT   MOD_RES         207
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   402 AA;  44938 MW;  1FEFCDD237D7992E CRC64;
     MSAKEKIYSI VAHDAHDDRH HGSINVPIYQ TSLFSFDTYE QFNLARLEEQ ENFVYSRGNN
     PTVRYLEDKL AQLEHGERAK CFSSGMAAIS AAIMSIVKQG DHVICTHQAY GPTREFLGVY
     LQKFGIETTF VDGSSLENWK SAVRPNTKLL YLESPTSMMF QLQDIRGCAE LALSIGAETI
     LDNSWATPCY QNPLTMGVGL VVHSITKYIS GHSDCVGGVV VGSKRLMDPL MSTEYMLFGG
     IMTPQTAGLV TRGLRTLPLR MQRHEMSGLK VAEYLCGQYF VVKVNHPGLT NHPQHEMART
     QMSGYGSLFS FESNVPVVKL RAWADRLQYF RIGASWGGFE SLINVNALNN SDQRSCSLVR
     LYIGTEDPDD LIRDLDEAWR CVAISPSEGE LYEQNPSFNQ NG
//