ID V4QKY7_9CAUL Unreviewed; 388 AA.
AC V4QKY7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ESQ79828.1};
GN ORFNames=AEYBE204_08255 {ECO:0000313|EMBL:ESQ79828.1};
OS Asticcacaulis sp. YBE204.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282363 {ECO:0000313|EMBL:ESQ79828.1, ECO:0000313|Proteomes:UP000017808};
RN [1] {ECO:0000313|EMBL:ESQ79828.1, ECO:0000313|Proteomes:UP000017808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YBE204 {ECO:0000313|EMBL:ESQ79828.1,
RC ECO:0000313|Proteomes:UP000017808};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ79828.1}.
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DR EMBL; AWGF01000004; ESQ79828.1; -; Genomic_DNA.
DR RefSeq; WP_023461945.1; NZ_AWGF01000004.1.
DR AlphaFoldDB; V4QKY7; -.
DR STRING; 1282363.AEYBE204_08255; -.
DR PATRIC; fig|1282363.3.peg.1634; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000017808; Unassembled WGS sequence.
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:ESQ79828.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000017808}.
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 388 AA; 42325 MW; BCF9CACFD0E6E8C9 CRC64;
MREITRLTSA TLDKPKSRRA VNVGVERGST VLMESAEFLY NDDIKPTYGT DGLSTQAELC
RLIADLEGAY KAFILPTGLA AQTLPIFAAL KAGDHVLAVN SAYAPVRRFL NTQMQRYGIS
ITWYAPSLSP EAVLDLAQDN TRLIYVESPG SLTFEIQDIP AIAALARARG ILTLCDNTYG
AGVLFKPLAH GCDVSMQALT KYAGGHSDVL MGSVAVNDPK LAKQIYDAIK AWGFFTSADE
SYLAIRGLRT LHLRLQRSGE SGLKVARWLE GRPEVLRVVH PALDSHKGSD VFNRDFTGPN
GLFLVVLKGD GEATSHRFLN ALKLFGLGFS WGGFESLAVN CEPQFLGRHK ITPEDHAPLE
GSYVRLYVGL EDPDDLIADI EQALNEIA
//
