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Database: UniProt
Entry: A0A0N0KBL4_9PROT
LinkDB: A0A0N0KBL4_9PROT
Original site: A0A0N0KBL4_9PROT 
ID   A0A0N0KBL4_9PROT        Unreviewed;       387 AA.
AC   A0A0N0KBL4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:KPF88218.1};
GN   ORFNames=IP70_00780 {ECO:0000313|EMBL:KPF88218.1};
OS   alpha proteobacterium AAP38.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1523418 {ECO:0000313|EMBL:KPF88218.1, ECO:0000313|Proteomes:UP000037884};
RN   [1] {ECO:0000313|EMBL:KPF88218.1, ECO:0000313|Proteomes:UP000037884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP38 {ECO:0000313|EMBL:KPF88218.1,
RC   ECO:0000313|Proteomes:UP000037884};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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|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:KPF88218.1}.
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DR   EMBL; LJHR01000003; KPF88218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0KBL4; -.
DR   STRING; 1523418.IP70_00780; -.
DR   PATRIC; fig|1523418.3.peg.2088; -.
DR   OrthoDB; 9790858at2; -.
DR   Proteomes; UP000037884; Unassembled WGS sequence.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
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:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 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:KPF88218.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         203
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   387 AA;  42238 MW;  9E072E99F7C32599 CRC64;
     MKDRPNRQGF ATRAIHAGQQ PDPTTGAIMV PIYATSTFVQ ESPGVHKGYE YARSQNPTRM
     AYEACIADLE SGYRGYAFAS GLAAEATILE LLDAGAHVIA SDDLYGGTYR LLHRVRSRTA
     NLSVTTVDLS DLDAVKAAIR PETRMIWVET PTNPLLKLAD LEALAQLAKT HNLISVADNT
     FASPWIQRPL EQGFDIVVHS ATKYLNGHSD MVGGVAVVRE AGEIADRMAF LHNAVGAIQG
     PFDSFLVMRS LKTLALRMER HCQNAVVIAE WLEKHPSVAK VRYPFLPSHA QHDLAKRQMR
     AGGGMVTIHL KGGLEPARRM LERTELFSLA ESLGGVESLI EHPAIMTHAS IPPEQRAAIG
     IDDGLVRLSV GVEDVNDLLA DLEQALR
//
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