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Entry: F2KHQ0_PSEBN
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ID   F2KHQ0_PSEBN            Unreviewed;       400 AA.
AC   F2KHQ0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Putative cystathionine gamma-lyase {ECO:0000313|EMBL:AEA69336.1};
GN   ORFNames=PSEBR_a3032 {ECO:0000313|EMBL:AEA69336.1};
OS   Pseudomonas brassicacearum (strain NFM421).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=994484 {ECO:0000313|EMBL:AEA69336.1, ECO:0000313|Proteomes:UP000006692};
RN   [1] {ECO:0000313|EMBL:AEA69336.1, ECO:0000313|Proteomes:UP000006692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NFM421 {ECO:0000313|EMBL:AEA69336.1,
RC   ECO:0000313|Proteomes:UP000006692};
RX   PubMed=21515771; DOI=10.1128/JB.00411-11;
RA   Ortet P., Barakat M., Lalaouna D., Fochesato S., Barbe V., Vacherie B.,
RA   Santaella C., Heulin T., Achouak W.;
RT   "Complete genome sequence of a beneficial plant root-associated bacterium,
RT   Pseudomonas brassicacearum.";
RL   J. Bacteriol. 193:3146-3146(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NFM421;
RA   Ortet P., Barakat M., Lalaouna D., Fochesato S., Barbe V., Santaella C.,
RA   Heulin T., Achouak W.;
RT   "Complete Genome Sequence of a beneficial plant roots-associated bacterium
RT   Pseudomonas brassicacearum.";
RL   Submitted (MAR-2011) 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; CP002585; AEA69336.1; -; Genomic_DNA.
DR   RefSeq; WP_013693449.1; NC_015379.1.
DR   AlphaFoldDB; F2KHQ0; -.
DR   STRING; 994484.PSEBR_a3032; -.
DR   KEGG; pba:PSEBR_a3032; -.
DR   HOGENOM; CLU_018986_2_0_6; -.
DR   Proteomes; UP000006692; Chromosome.
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:SF90; 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:AEA69336.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         213
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   400 AA;  43382 MW;  A37F8CA7E6D4C0C8 CRC64;
     MRPDKHNLST LSAATLAVHG GNVADVTSGA VRTPLVMANS YLLPEDPATM DWSSPDGLVY
     TRNQGHNQVC LEKKLAALEG CGDAVVFATG VAALHSVFFS FLKSGDHVIV SDITYQAVWR
     LFAELLPERY GIEATFVDVG DLESVRNAIR PNTKLIHTET IANPTTKVAD IAALAEIAHA
     HGALISVDAT FTPPPFFRAS EHGVDFVIHS LTKYINGHGD AMGGVVIGSN QLINKIKNDA
     LVDLGATISP FNAWMIMRGS VTLPLRLTQL LNTAEKLAQF LEGDDRIAYV YYPGLPSHPQ
     HELARRQFAG KGYGAVMAFA VEGDPDTQNR FVSNLRIITS AVSLGHDESL IVHVGAEGRG
     GFDKYPEEFR QYGHLRFSVG LEDPDDLIKD ITFALDATFN
//
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