ID A0A0M2KLT5_9GAMM Unreviewed; 399 AA.
AC A0A0M2KLT5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:KKF37951.1};
DE EC=4.4.1.8 {ECO:0000313|EMBL:KKF37951.1};
GN ORFNames=SY86_21820 {ECO:0000313|EMBL:KKF37951.1};
OS Erwinia tracheiphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=65700 {ECO:0000313|EMBL:KKF37951.1, ECO:0000313|Proteomes:UP000033924};
RN [1] {ECO:0000313|EMBL:KKF37951.1, ECO:0000313|Proteomes:UP000033924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BuffGH {ECO:0000313|EMBL:KKF37951.1,
RC ECO:0000313|Proteomes:UP000033924};
RA Shapiro L.R.;
RT "Erwinia tracheiphila.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KKF37951.1}.
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DR EMBL; JXNU01000003; KKF37951.1; -; Genomic_DNA.
DR RefSeq; WP_016190437.1; NZ_JXNU01000003.1.
DR AlphaFoldDB; A0A0M2KLT5; -.
DR STRING; 65700.SY86_21820; -.
DR PATRIC; fig|65700.7.peg.5433; -.
DR Proteomes; UP000033924; 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 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 Lyase {ECO:0000313|EMBL:KKF37951.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000033924}.
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 399 AA; 43503 MW; E2501BBCC3143F35 CRC64;
MNSKKIETAL ITAGRNKRYT QGAVNSVIQR ASSLVFDTVA DKKRATAGRA DGELFYGRRG
TLTHFSLQDA MTELEGGAGC VLYPCGAAAV ANAILAFVSA GDNVLMAGSV YEPTQDFCSK
ILSKMNVSTT WFSHCSGAEI AQQVQPETRV VFLESPASIT MEIQDIPAIV AAVRSKSPEA
VIIMDNTWAA GILFPALKYG IDISVQAGTK YLIGHSDAMI GTAVASQRCW PQLRENSYLM
GQMVDADTAY MASRGLRTLA VRLRQHQESA LQIANWLSDR PEVAVVNHPA LPQCRGHQFW
KRDFTGSSGL FSFVLRMRLD DQQLAAYLDH FQHFSMAYSW GGFESLILAN QPDELAAIRP
AGSIDFSGTL IRVHIGLENV DDLIADLAAG FERLAWLSI
//
