ID B4R9W1_PHEZH Unreviewed; 398 AA.
AC B4R9W1;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ACG77875.1};
GN OrderedLocusNames=PHZ_c1462 {ECO:0000313|EMBL:ACG77875.1};
OS Phenylobacterium zucineum (strain HLK1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG77875.1, ECO:0000313|Proteomes:UP000001868};
RN [1] {ECO:0000313|EMBL:ACG77875.1, ECO:0000313|Proteomes:UP000001868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLK1 {ECO:0000313|EMBL:ACG77875.1,
RC ECO:0000313|Proteomes:UP000001868};
RX PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT "Complete genome of Phenylobacterium zucineum - a novel facultative
RT intracellular bacterium isolated from human erythroleukemia cell line
RT K562.";
RL BMC Genomics 9:386-386(2008).
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; CP000747; ACG77875.1; -; Genomic_DNA.
DR RefSeq; WP_012522019.1; NC_011144.1.
DR AlphaFoldDB; B4R9W1; -.
DR STRING; 450851.PHZ_c1462; -.
DR KEGG; pzu:PHZ_c1462; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_5_1_5; -.
DR OrthoDB; 9790858at2; -.
DR Proteomes; UP000001868; Chromosome.
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 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:ACG77875.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001868}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 398 AA; 42477 MW; 02155A9B96121CFA CRC64;
MRDPTLCLTP GDGLGGAFES LAVPVHRAST VVFPTVAAYQ GRRDEIYDGF SYGLYGTPTS
RELETRLARL EGAARTLALP SGFAAIAMTT LAAVRPGEEV LFPDTTYDTV RPFAERFLAG
LGIGSRYYDP MIGAGLAEVL DGGTRLVWVE SPGSMTMEVQ DVPAIAAAAH ARGAMVAADN
TWATPLRFKA LAHGVDFSVC ALSKYVAGHS DVMMGSVSVN DVGLYRKLKD YSRFLGLGVS
ADESSLVLRG LETLAIRMDR AEQSARRLVD WVVAQPGVAE VRFPQLATSP GHALWRRDFT
GGAGLFSVFL EDWTRPALAE AVESLQLFAI GASWGGTRSL VAVLDRPPLR TVAPPAHTGP
VVRFSIGLED PEDLLQDLAR GFARLAAPDQ GGGAQRRA
//
