ID G0ETJ3_CUPNN Unreviewed; 407 AA.
AC G0ETJ3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Cystathionine beta-lyase MetC {ECO:0000313|EMBL:AEI76819.1};
DE EC=4.4.1.8 {ECO:0000313|EMBL:AEI76819.1};
GN Name=metC1 {ECO:0000313|EMBL:AEI76819.1};
GN OrderedLocusNames=CNE_1c14730 {ECO:0000313|EMBL:AEI76819.1};
OS Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS / N-1) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI76819.1, ECO:0000313|Proteomes:UP000006798};
RN [1] {ECO:0000313|EMBL:AEI76819.1, ECO:0000313|Proteomes:UP000006798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1
RC {ECO:0000313|Proteomes:UP000006798};
RX PubMed=21742890; DOI=10.1128/JB.05660-11;
RA Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL J. Bacteriol. 193:5017-5017(2011).
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; CP002877; AEI76819.1; -; Genomic_DNA.
DR RefSeq; WP_013956459.1; NC_015726.1.
DR AlphaFoldDB; G0ETJ3; -.
DR KEGG; cnc:CNE_1c14730; -.
DR HOGENOM; CLU_018986_5_1_4; -.
DR Proteomes; UP000006798; 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 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AEI76819.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 217
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 407 AA; 44388 MW; 8834501A220A1C03 CRC64;
MSDSPSDKPA SPAHYLQTVA VQPELEIAPG FASFSPATHR GSTVVFRNLA ELRAHGDGAT
TYWRYGLHAT PTSEALCQHL ALLEGARHTL LQPSGLAAIS LVYFALLKSG DDVLVPRNVY
GPNRDHGEWL AREFGVTVRY YDPMDAAAVA AMIRPNTRLV WMESPGSVTM EVPDSDAIVA
AARARGVLTA IDNTWSAGIY FRPFDKGIDI SVQALTKYQS GGSDVLMGAV LTCDDALHER
LKRTRMLMGW GVSADDCHLV LRGLPSLPVR LAAHDRAARE VAEWLHQRPE VSRVLHPALP
DCPGHASWRR DFTGASGLFA IILRASYTRQ QVDAFVEALQ LFAIGWSWGG AHSLAVPYHV
QGMRPAGTWP PAGWQDTGEL VRLYIGLEDT RDLIADLRQA LEATLAA
//
