METC_RHIL3
ID METC_RHIL3 Reviewed; 396 AA.
AC Q52811; Q1MH70;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Putative cystathionine beta-lyase;
DE Short=CBL;
DE EC=4.4.1.13 {ECO:0000250|UniProtKB:P06721};
DE AltName: Full=Beta-cystathionase;
DE AltName: Full=Cysteine lyase;
DE AltName: Full=Cysteine-S-conjugate beta-lyase;
DE AltName: Full=ORF5;
GN Name=metC; OrderedLocusNames=RL2205;
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-117.
RX PubMed=8898392; DOI=10.1046/j.1365-2958.1996.00078.x;
RA Walshaw D.L., Poole P.S.;
RT "The general L-amino acid permease of Rhizobium leguminosarum is an ABC
RT uptake system that also influences efflux of solutes.";
RL Mol. Microbiol. 21:1239-1252(1996).
CC -!- FUNCTION: Catalyzes the cleavage of cystathionine to homocysteine,
CC pyruvate and ammonia during methionine biosynthesis.
CC {ECO:0000250|UniProtKB:P06721}.
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:0000250|UniProtKB:P06721};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC Evidence={ECO:0000250|UniProtKB:P06721};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P06721};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homocysteine from L-cystathionine: step 1/1.
CC {ECO:0000250|UniProtKB:P06721}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AM236080; CAK07697.1; -; Genomic_DNA.
DR EMBL; X82596; CAA57932.1; -; Genomic_DNA.
DR RefSeq; WP_011651802.1; NC_008380.1.
DR AlphaFoldDB; Q52811; -.
DR SMR; Q52811; -.
DR STRING; 216596.RL2205; -.
DR EnsemblBacteria; CAK07697; CAK07697; RL2205.
DR KEGG; rle:RL2205; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_5_1_5; -.
DR OMA; GPYTYGR; -.
DR OrthoDB; 637281at2; -.
DR UniPathway; UPA00051; UER00078.
DR Proteomes; UP000006575; Chromosome.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR43500; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01324; cysta_beta_ly_B; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Lyase; Methionine biosynthesis;
KW Pyridoxal phosphate.
FT CHAIN 1..396
FT /note="Putative cystathionine beta-lyase"
FT /id="PRO_0000114771"
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P06721"
SQ SEQUENCE 396 AA; 43004 MW; 33C516CF75DD23B8 CRC64;
MKDKDSLLQN AGINTRLTHI GNDPFDYHGF INPPVVHAST VLFPNARAME TRTQKYTYGT
RGTPTTDALC EAIDALEGSA GTILVPSGLA AVTIPFLGFV AAGDHALVVD SVYGPTRHFC
DTMLKRLGVE VEYYHPEIGA GIETLFRSNT KLVHTEAPGS NTFEMQDIPA ISAVAHRHGA
VVMMDNTWAT PVYFRPLDHG VDISIHASTK YPSGHSDILL GTVSANAEHW ERLKEANGVL
GICGAPDDAY QILRGLRTMG LRLERHYESA LDIAKWLEGR DDVARVLHPA LPSFPSHHLW
KRDFKGASGI FSFVLAADGP EKSRAKAHAF LDALRIFGLG YSWGGFESLA LHAYLNDRTV
AKAPTDGPVI RLQIGIEDVA DLKADIERGF AAASAV
