METC_HAEIN
ID METC_HAEIN Reviewed; 396 AA.
AC P44527;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=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;
GN Name=metC; OrderedLocusNames=HI_0122;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P06721}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06721}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC21796.1; -; Genomic_DNA.
DR PIR; E64049; E64049.
DR RefSeq; NP_438294.1; NC_000907.1.
DR RefSeq; WP_005694414.1; NC_000907.1.
DR AlphaFoldDB; P44527; -.
DR SMR; P44527; -.
DR STRING; 71421.HI_0122; -.
DR EnsemblBacteria; AAC21796; AAC21796; HI_0122.
DR KEGG; hin:HI_0122; -.
DR PATRIC; fig|71421.8.peg.126; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_5_1_6; -.
DR OMA; GPYTYGR; -.
DR PhylomeDB; P44527; -.
DR BioCyc; HINF71421:G1GJ1-132-MON; -.
DR UniPathway; UPA00051; UER00078.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IBA:GO_Central.
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:0019450; P:L-cysteine catabolic process to pyruvate; IBA:GO_Central.
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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Lyase; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..396
FT /note="Cystathionine beta-lyase"
FT /id="PRO_0000114770"
FT MOD_RES 211
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P06721"
SQ SEQUENCE 396 AA; 44345 MW; 5ABFD4A3C4F991EE CRC64;
MQTKYDLSTM FIHSGRQKRF SQGSVNPVLQ RASSLLFDSI EDKKHATQRR AKGELFYGRR
GTLTHFALQD LMCEMEGGAG CYLYPCGTAA VTNSILSFVK TGDHVLMSGA AYEPTQYFCN
IVLKKMQIDI TYYDPLIGED IATLIQPNTK VLFLEAPSSI TMEIPDIPTI VKAARKVNPN
IVIMIDNTWS AGVLFKALEH DIDISIQAGT KYLVGHSDIM IGTAVANART WDQLREHSYL
MGQMVDADSA YTTARGIRTL GVRLKQHQES SIKVAKWLSE QPEVKTVYHP ALPSCPGHEF
FLRDFSGSSG LFSFELTQRL TSEQVSKFMD HFQLFAMAYS WGGFESLILC NQPEEIAHIR
PNIKRNLTGS LIRVHIGFEN VDELIADLKA GFERIA
