ID A0A0H3C825_CAUVN Unreviewed; 386 AA.
AC A0A0H3C825;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ACL94956.1};
DE EC=4.4.1.8 {ECO:0000313|EMBL:ACL94956.1};
GN OrderedLocusNames=CCNA_01491 {ECO:0000313|EMBL:ACL94956.1};
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050 {ECO:0000313|EMBL:ACL94956.1, ECO:0000313|Proteomes:UP000001364};
RN [1] {ECO:0000313|EMBL:ACL94956.1, ECO:0000313|Proteomes:UP000001364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N {ECO:0000313|Proteomes:UP000001364};
RX PubMed=20472802; DOI=10.1128/JB.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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; CP001340; ACL94956.1; -; Genomic_DNA.
DR RefSeq; WP_010919300.1; NC_011916.1.
DR RefSeq; YP_002516864.1; NC_011916.1.
DR AlphaFoldDB; A0A0H3C825; -.
DR SMR; A0A0H3C825; -.
DR GeneID; 7333165; -.
DR KEGG; ccs:CCNA_01491; -.
DR PATRIC; fig|565050.3.peg.1469; -.
DR HOGENOM; CLU_018986_5_1_5; -.
DR OrthoDB; 9790858at2; -.
DR PhylomeDB; A0A0H3C825; -.
DR Proteomes; UP000001364; Chromosome.
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:ACL94956.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001364}.
FT MOD_RES 200
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 386 AA; 41270 MW; C85B0D4E4AF7E887 CRC64;
MDEETRLIHT GSEPARLGRT VNPPIQRGST VLLPDAASLY DDDQLTYGIT GLSTPVALQN
ALAELEGATN VTLYPSGLAA ITGAMLAVLK AGDEVLVVDS AYKPTRRFCD RVLGRFGVTT
RYYDPKLSPE ALMGLVTSST RLIVLEAPGS LTFEMQDIPA IAAAANARGV LTLIDNTWAA
GLLFKPLAHG VTMSVQALTK YVGGHSDCFM GSVATCDDAV AKLLGDAMWD IGWSVSSDDA
YTMLRGLRTL ATRLPRHAEN GLAIARWLQE RPEVARVLHP ALPGDAGHAI WKRDFTGACG
LFGVVLKPCS QKAVHAFLDS LKLFGLGFSW GGYESLALNC DPQLGARSIP VDLEGPLLRF
HIGLEGIEDL KADLRRGFEA LNAAKA
//
