Q08432 (CBL_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cystathionine beta-lyase PatB
Short name=CBL
EC=4.4.1.8

Alternative name(s):
Beta-cystathionase
Cysteine lyase

Gene names

Name:	patB
Ordered Locus Names:	BSU31440

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transformation of cystathionine to homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine.
Catalytic activity	L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate. Ref.4
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
Induction	Constitutively expressed at a low level. Ref.4
Disruption phenotype	No visible phenotype. Ref.4
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
Biophysicochemical properties	Kinetic parameters: KM=1.62 mM for cystathionine Ref.4

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cystathionine beta-lyase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 387	387	Cystathionine beta-lyase PatB		PRO_0000163848
Amino acid modifications
	Modified residue	234	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q08432 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 959A4B1C500D5CFB	FASTA	387	42,789
	10 20 30 40 50 60 MNFDKREERL GTQSVKWDKT GELFGVTDAL PMWVADMDFR APEAITEALK ERLDHGIFGY 70 80 90 100 110 120 TTPDQKTKDA VCGWMQNRHG WKVNPESITF SPGVVTALSM AVQAFTEPGD QVVVQPPVYT 130 140 150 160 170 180 PFYHMVEKNG RHILHNPLLE KDGAYAIDFE DLETKLSDPS VTLFILCNPH NPSGRSWSRE 190 200 210 220 230 240 DLLKLGELCL EHGVTVVSDE IHSDLMLYGH KHTPFASLSD DFADISVTCA APSKTFNIAG 250 260 270 280 290 300 LQASAIIIPD RLKRAKFSAS LQRNGLGGLN AFAVTAIEAA YSKGGPWLDE LITYIEKNMN 310 320 330 340 350 360 EAEAFLSTEL PKVKMMKPDA SYLIWLDFSA YGLSDAELQQ RMLKKGKVIL EPGTKYGPGG 370 380 EGFMRLNAGC SLATLQDGLR RIKAALS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Multisensory activation of the phosphorelay initiating sporulation in Bacillus subtilis: identification and sequence of the protein kinase of the alternate pathway." Trach K.A., Hoch J.A. Mol. Microbiol. 8:69-79(1993) [PubMed: 8497199] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai)." Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H., Duesterhoeft A., Pohl T.M., Weitzenegger T. Microbiology 143:2769-2774(1997) [PubMed: 9274030] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"The PatB protein of Bacillus subtilis is a C-S-lyase." Auger S., Gomez M.P., Danchin A., Martin-Verstraete I. Biochimie 87:231-238(2005) [PubMed: 15760717] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, DISRUPTION PHENOTYPE. Strain: 168.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U63302 Genomic DNA. Translation: AAB61979.1. Z93933 Genomic DNA. Translation: CAB07910.1. Z93934 Genomic DNA. Translation: CAB07924.1. AL009126 Genomic DNA. Translation: CAB15133.1.
PIR	S32934.
RefSeq	NP_391022.1. NC_000964.3.
3D structure databases
ProteinModelPortal	Q08432.
SMR	Q08432. Positions 2-387.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000002936; EBBACP00000002936; EBBACG00000002930.
GeneID	937170.
GenomeReviews	Gene locus BSU31440 in contig AL009126_GR.
KEGG	bsu:BSU31440.
NMPDR	fig|224308.1.peg.3147.
PATRIC	18978256. VBIBacSub10457_3291.
Organism-specific databases
GenoList	BSU31440. [Micado]
Phylogenomic databases
GeneTree	EBGT00070000031804.
HOGENOM	HBG681988.
OMA	IHSDLML.
PhylomeDB	Q08432.
ProtClustDB	CLSK887791.
Enzyme and pathway databases
BioCyc	BSUB:BSU31440-MONOMER.
Family and domain databases
InterPro	IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KO	K14155.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CBL_BACSU

Accession

Primary (citable) accession number: Q08432

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program