CBL_BACSU
ID CBL_BACSU Reviewed; 387 AA.
AC Q08432;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cystathionine beta-lyase PatB;
DE Short=CBL;
DE EC=4.4.1.13;
DE AltName: Full=Beta-cystathionase PatB;
DE AltName: Full=Cysteine lyase PatB;
DE AltName: Full=Cysteine-S-conjugate beta-lyase PatB {ECO:0000305};
GN Name=patB; OrderedLocusNames=BSU31440;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8497199; DOI=10.1111/j.1365-2958.1993.tb01204.x;
RA Trach K.A., Hoch J.A.;
RT "Multisensory activation of the phosphorelay initiating sporulation in
RT Bacillus subtilis: identification and sequence of the protein kinase of the
RT alternate pathway.";
RL Mol. Microbiol. 8:69-79(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9274030; DOI=10.1099/00221287-143-8-2769;
RA Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H.,
RA Duesterhoeft A., Pohl T.M., Weitzenegger T.;
RT "Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence
RT of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).";
RL Microbiology 143:2769-2774(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=15760717; DOI=10.1016/j.biochi.2004.09.007;
RA Auger S., Gomez M.P., Danchin A., Martin-Verstraete I.;
RT "The PatB protein of Bacillus subtilis is a C-S-lyase.";
RL Biochimie 87:231-238(2005).
CC -!- FUNCTION: Catalyzes the transformation of cystathionine to
CC homocysteine. Also exhibits cysteine desulfhydrase activity in vitro,
CC producing sulfide from cysteine.
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:0000269|PubMed:15760717};
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.62 mM for cystathionine {ECO:0000269|PubMed:15760717};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homocysteine from L-cystathionine: step 1/1.
CC -!- INDUCTION: Constitutively expressed at a low level.
CC {ECO:0000269|PubMed:15760717}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:15760717}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
CC {ECO:0000305}.
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DR EMBL; U63302; AAB61979.1; -; Genomic_DNA.
DR EMBL; Z93933; CAB07910.1; -; Genomic_DNA.
DR EMBL; Z93934; CAB07924.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15133.1; -; Genomic_DNA.
DR PIR; S32934; S32934.
DR RefSeq; NP_391022.1; NC_000964.3.
DR RefSeq; WP_003228854.1; NZ_JNCM01000033.1.
DR PDB; 6QP3; X-ray; 2.30 A; A/B/C/D=1-387.
DR PDBsum; 6QP3; -.
DR AlphaFoldDB; Q08432; -.
DR SMR; Q08432; -.
DR STRING; 224308.BSU31440; -.
DR jPOST; Q08432; -.
DR PaxDb; Q08432; -.
DR PRIDE; Q08432; -.
DR EnsemblBacteria; CAB15133; CAB15133; BSU_31440.
DR GeneID; 937170; -.
DR KEGG; bsu:BSU31440; -.
DR PATRIC; fig|224308.179.peg.3408; -.
DR eggNOG; COG1168; Bacteria.
DR InParanoid; Q08432; -.
DR OMA; RINIGCP; -.
DR PhylomeDB; Q08432; -.
DR BioCyc; BSUB:BSU31440-MON; -.
DR SABIO-RK; Q08432; -.
DR UniPathway; UPA00051; UER00078.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:RHEA.
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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR027619; C_S_lyase_PatB.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR04350; C_S_lyase_PatB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Lyase; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..387
FT /note="Cystathionine beta-lyase PatB"
FT /id="PRO_0000163848"
FT MOD_RES 234
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:6QP3"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:6QP3"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6QP3"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:6QP3"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 121..127
FT /evidence="ECO:0007829|PDB:6QP3"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:6QP3"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:6QP3"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:6QP3"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:6QP3"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:6QP3"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:6QP3"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:6QP3"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:6QP3"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 285..309
FT /evidence="ECO:0007829|PDB:6QP3"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:6QP3"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 335..344
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:6QP3"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:6QP3"
FT HELIX 372..385
FT /evidence="ECO:0007829|PDB:6QP3"
SQ SEQUENCE 387 AA; 42789 MW; 959A4B1C500D5CFB CRC64;
MNFDKREERL GTQSVKWDKT GELFGVTDAL PMWVADMDFR APEAITEALK ERLDHGIFGY
TTPDQKTKDA VCGWMQNRHG WKVNPESITF SPGVVTALSM AVQAFTEPGD QVVVQPPVYT
PFYHMVEKNG RHILHNPLLE KDGAYAIDFE DLETKLSDPS VTLFILCNPH NPSGRSWSRE
DLLKLGELCL EHGVTVVSDE IHSDLMLYGH KHTPFASLSD DFADISVTCA APSKTFNIAG
LQASAIIIPD RLKRAKFSAS LQRNGLGGLN AFAVTAIEAA YSKGGPWLDE LITYIEKNMN
EAEAFLSTEL PKVKMMKPDA SYLIWLDFSA YGLSDAELQQ RMLKKGKVIL EPGTKYGPGG
EGFMRLNAGC SLATLQDGLR RIKAALS
