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Database: UniProt
Entry: A0A1E3L7J9_9BACL
LinkDB: A0A1E3L7J9_9BACL
Original site: A0A1E3L7J9_9BACL 
ID   A0A1E3L7J9_9BACL        Unreviewed;       388 AA.
AC   A0A1E3L7J9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ODP28940.1};
DE            EC=4.4.1.8 {ECO:0000313|EMBL:ODP28940.1};
GN   Name=metC {ECO:0000313|EMBL:ODP28940.1};
GN   ORFNames=PTI45_01449 {ECO:0000313|EMBL:ODP28940.1};
OS   Paenibacillus nuruki.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1886670 {ECO:0000313|EMBL:ODP28940.1, ECO:0000313|Proteomes:UP000094578};
RN   [1] {ECO:0000313|EMBL:ODP28940.1, ECO:0000313|Proteomes:UP000094578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TI45-13ar {ECO:0000313|EMBL:ODP28940.1,
RC   ECO:0000313|Proteomes:UP000094578};
RA   Kim S.-J.;
RT   "Genome sequencing of Paenibacillus sp. TI45-13ar, isolated from Korean
RT   traditional nuruk.";
RL   Submitted (AUG-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}.
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:ODP28940.1}.
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DR   EMBL; MDER01000032; ODP28940.1; -; Genomic_DNA.
DR   RefSeq; WP_069326894.1; NZ_MDER01000032.1.
DR   AlphaFoldDB; A0A1E3L7J9; -.
DR   STRING; 1886670.PTI45_01449; -.
DR   PATRIC; fig|1886670.3.peg.1477; -.
DR   Proteomes; UP000094578; Unassembled WGS sequence.
DR   GO; GO:0004121; F:cystathionine 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   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:SF15; CYSTATHIONINE GAMMA-LYASE; 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.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:ODP28940.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094578}.
FT   MOD_RES         205
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   388 AA;  41960 MW;  D9762572F0D9B5CE CRC64;
     MAYSSDHSSS RKIDTKLIHF GAAFDKATGA SSVPIYQAST FHQEDISNPP LHDYSRSGNP
     TRQALEDYIA LLEGGAKGYA FASGMAAIST AFLILSAGDH VIVTEDVYGG TYRFLTTVLN
     RMNIEISFVD MTDLDQVKHA LRPNTRAVYM ETPSNPTLKI TDIGAVTAWA KEHHLLTMVD
     NTFMTPYYQR PIEMGVDIVL HSATKFLGGH SDVLAGLAVA RTPEIGAQLK HLQNGLGTVL
     GPQDCWLLIR GMKTLAARMN HSEKSTAKLA QWLNERDDIE AVYYPGLESH PGATIHASQS
     SGAGSVLSFD VGSGERAKKV LDNVQIPLVA VSLGAVESIL SYPATMSHAA MGEGVRKERG
     ITDGLLRFSV GLEDIDDLIA DLEQALQE
//
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