ID U5N9I1_9BURK Unreviewed; 407 AA.
AC U5N9I1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:AGX88067.1};
GN Name=metC {ECO:0000313|EMBL:AGX88067.1};
GN ORFNames=Cenrod_1994 {ECO:0000313|EMBL:AGX88067.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX88067.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX88067.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX88067.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(2013).
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; CP004885; AGX88067.1; -; Genomic_DNA.
DR RefSeq; WP_022774892.1; NC_022576.1.
DR AlphaFoldDB; U5N9I1; -.
DR STRING; 946483.Cenrod_1994; -.
DR KEGG; cbx:Cenrod_1994; -.
DR PATRIC; fig|946483.4.peg.2008; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_5_1_4; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000017184; 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 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:AGX88067.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000017184}.
FT MOD_RES 213
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 407 AA; 44245 MW; 8A5DF3D3B2E27F33 CRC64;
MTTPRTQLIH HRYEPPAGFS APQPGVHKAS TVFFSSVEAL RSIRWKDRSA YTYGLHGTPT
TYTLEERLCT LEGGRYCVLT PSGLSAITLV FLAMLRTGDE VLLPWNTYSP AVAFAQQELL
RWGITHQFYD PLRPEDLAQR IRASTRLVWI EAAGSVTLEF PDLPALVRIC LDAGVRCALD
DTWSAGQAYA PFDLLPGTTP ALGVDIALSA LTKYHSGGGD ILMGSLITVD ADLHERLSLC
HMRLGLGVGA NDVEAVLRGL PTLAVRYAAQ DEAARTLAVW CQSRPEFAQV LHPALPGSPG
HAHWLALCHG NGSRAGRAAG LFAVVFRADI PQASVDAFCN ALQYFRIGYS WGGPVSLVMP
YDLPPERRQS SPHLASGCLV RFAIGFEDVA DLQADLSRAL GQCLQPR
//
