ID E0TDW7_PARBH Unreviewed; 381 AA.
AC E0TDW7;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ADM10416.1};
GN OrderedLocusNames=PB2503_11859 {ECO:0000313|EMBL:ADM10416.1};
OS Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 / KCTC 12087).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC Parvularculaceae; Parvularcula.
OX NCBI_TaxID=314260 {ECO:0000313|EMBL:ADM10416.1, ECO:0000313|Proteomes:UP000001302};
RN [1] {ECO:0000313|Proteomes:UP000001302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC {ECO:0000313|Proteomes:UP000001302};
RA Kang D.-M., Oh H.-M., Cho J.-C.;
RT "Genome sequence of Parvularcula bermudensis HTCC2503.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADM10416.1, ECO:0000313|Proteomes:UP000001302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC {ECO:0000313|Proteomes:UP000001302};
RX PubMed=21037002; DOI=10.1128/JB.01205-10;
RA Oh H.M., Kang I., Vergin K.L., Kang D., Rhee K.H., Giovannoni S.J.,
RA Cho J.C.;
RT "Complete genome sequence of strain HTCC2503T of Parvularcula bermudensis,
RT the type species of the order "Parvularculales" in the class
RT Alphaproteobacteria.";
RL J. Bacteriol. 193:305-306(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}.
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DR EMBL; CP002156; ADM10416.1; -; Genomic_DNA.
DR RefSeq; WP_013301390.1; NC_014414.1.
DR AlphaFoldDB; E0TDW7; -.
DR STRING; 314260.PB2503_11859; -.
DR KEGG; pbr:PB2503_11859; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_5_1_5; -.
DR OrthoDB; 9790858at2; -.
DR Proteomes; UP000001302; 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:ADM10416.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001302}.
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 381 AA; 40841 MW; 0EC891A6BEE903F9 CRC64;
MKGPTKDTHL GRPTKGRRLI NPSVECGSTV LFSSYDDFRA NRPPWHYGRT GTPTHRALEE
SLCDLEGADN VVLTGSGLEA CTLAILSCVT AGGHVLVTDS AYEPTRTFCD GLLRGFDIET
TYFDPQAGRE EIAALCRPTT QLIFCESPGS LTFEVQDLPA IVAGAGEVPV AVDNTYGAGV
LLRPLELGCA ISVQALTKYV GGHSDLLLGA VATAPRLSAK VRRMARMLGI SVSGRDVAMA
HRGLRTLHRR LAVHEENGLG LARFLETHSA IRRVLHPGLD SHPQAALWAR DASGTNGLFS
VIADWEDEAV TARFIDHLTL FGLGYSWGGY ESLCLPAWPT ANRTAVPWTE GGQVLRFHAG
LEDLDDLIED VAAALAAATS T
//