ID A0A239S7H8_9BURK Unreviewed; 417 AA.
AC A0A239S7H8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:SNU80858.1};
DE EC=4.4.1.8 {ECO:0000313|EMBL:SNU80858.1};
GN Name=metC_1 {ECO:0000313|EMBL:SNU80858.1};
GN ORFNames=SAMEA4530655_00041 {ECO:0000313|EMBL:SNU80858.1};
OS Pandoraea sputorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=93222 {ECO:0000313|EMBL:SNU80858.1, ECO:0000313|Proteomes:UP000215126};
RN [1] {ECO:0000313|EMBL:SNU80858.1, ECO:0000313|Proteomes:UP000215126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13161 {ECO:0000313|EMBL:SNU80858.1,
RC ECO:0000313|Proteomes:UP000215126};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT906435; SNU80858.1; -; Genomic_DNA.
DR RefSeq; WP_039394388.1; NZ_LT906435.1.
DR AlphaFoldDB; A0A239S7H8; -.
DR STRING; 93222.NA29_04530; -.
DR KEGG; pspu:NA29_04530; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000215126; Chromosome 1.
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; 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:SNU80858.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 417 AA; 45070 MW; 24D6C6747EA03423 CRC64;
MSRQSPPPSS PSASTPLAEH DAPHHGRSVR VATRLVKGGT DTAVIGGRAV NPPVVRASTV
LFESMDDMND ARRRRGTERM FTYGARGNPT GFALEDVVAG LEGGYRARLF PTGLAAITMV
FLAYVRPGDH VLIADCVYQP LRHFVETFLK PWGVHVTFFR ADGSDAAEHM TARTKMIYVE
APGSLVYEMC DIPALADLAH RHGALLVADN TWGSGVQCRP LMLGADISVM AATKYLSGHS
DVMMGTVTTT QEVWQTLSTM ADAQGVAVSP DDAYLVLRGT RTLAARLAMH ERNALEVAHW
LEGLPDVARV FCLALPTDPG HALWRRDCLG TNGLVSFEFA NATPVQADRF VDSLKLFGIG
ASWGGFESLA TVSNVVGTRT CEDWSHAGLI VRLHIGLEDP QDLIDDLAAA FEKVFGK
//
