ID Q6LK53_PHOPR Unreviewed; 395 AA.
AC Q6LK53;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:CAG22327.1};
GN Name=S3256 {ECO:0000313|EMBL:CAG22327.1};
GN OrderedLocusNames=PBPRB0454 {ECO:0000313|EMBL:CAG22327.1};
OS Photobacterium profundum (strain SS9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG22327.1, ECO:0000313|Proteomes:UP000000593};
RN [1] {ECO:0000313|Proteomes:UP000000593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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}.
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DR EMBL; CR378676; CAG22327.1; -; Genomic_DNA.
DR RefSeq; WP_011220536.1; NC_006371.1.
DR AlphaFoldDB; Q6LK53; -.
DR STRING; 298386.PBPRB0454; -.
DR KEGG; ppr:PBPRB0454; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_5_1_6; -.
DR Proteomes; UP000000593; Chromosome 2.
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 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; IPR006233; Cys_b_lyase_bac.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01324; cysta_beta_ly_B; 1.
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 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000593}.
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 395 AA; 44196 MW; E8046AEDDA1575B2 CRC64;
MEKKALDTKI ITAGRSKKWT QHLVNPPVSR ASTIVFDTVA EMKHATANRA NKELFYGRRG
TNTHFAFQDA MVELEGGVGC ALYPCGTAAI SNAILSFVKT GDHILMVDGT YEPTRDFCDK
ILDKMGVETT YYDPMVGEGI RDLIRPNTTV LFLESPCSIT MEVQDVPLLA SIAHEHDIVV
MLDNTWASPI NFQPFDHGVD ISIQAATKYI VGHSDVMLGT ATANERCWDQ LREGSYLMGQ
CTSPDDVYLA MRGLRTLGVR LRQHEKNSIK VAQWLSEREE VDHVRHPAFE SCEGHEIYKR
DFKGCNGLFS LVLKRGNTAA LTALLDGMEH FSMGYSWGGF ESLILANENV NSIRTAKKKE
FVGPMLRLHV GLEDVDDLIR DLEKGFERFN AVLEQ
//
