Cystathionine gamma-lyase - Bacillus subtilis

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O05394 (MCCB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cystathionine gamma-lyase
EC=4.4.1.1

Alternative name(s):
Gamma-cystathionase
Homocysteine gamma-lyase
EC=4.4.1.2

Gene names

Name:	mccB
Synonyms:	yrhB
Ordered Locus Names:	BSU27250

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of cystathionine to cysteine, and homocysteine to sulfide. Ref.3
Catalytic activity	L-cystathionine + H₂O = L-cysteine + NH₃ + 2-oxobutanoate. Ref.3 L-homocysteine + H₂O = H₂S + NH₃ + 2-oxobutanoate. Ref.3
Cofactor	Pyridoxal phosphate By similarity.
Induction	By methionine. Repressed by sulfate and cysteine. Ref.3
Disruption phenotype	No visible phenotype. Ref.3
Sequence similarities	Belongs to the trans-sulfuration enzymes family.
Biophysicochemical properties	Kinetic parameters: K_M=3 mM for cystathionine Ref.3 V_max=2 µmol/min/mg enzyme for cystathionine gamma-lyase reaction

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	L-cysteine desulfhydrase activity Inferred from electronic annotation. Source: EC cystathionine gamma-lyase activity Inferred from electronic annotation. Source: EC homocysteine desulfhydrase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding 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 – 379

379

Cystathionine gamma-lyase

PRO_0000360652

Amino acid modifications

Modified residue

195

N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O05394 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 44DD71446F6E15B4
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FASTA

379

40,886

        10         20         30         40         50         60 
MKKKTLMIHG GITGDEKTGA VSVPIYQVST YKQPKAGQHT GYEYSRTANP TRTALEALVT 

        70         80         90        100        110        120 
ELESGEAGYA FSSGMAAITA VMMLFNSGDH VVLTDDVYGG TYRVMTKVLN RLGIESTFVD 

       130        140        150        160        170        180 
TSSREEVEKA IRPNTKAIYI ETPTNPLLKI TDLTLMADIA KKAGVLLIVD NTFNTPYFQQ 

       190        200        210        220        230        240 
PLTLGADIVL HSATKYLGGH SDVVGGLVVT ASKELGEELH FVQNSTGGVL GPQDSWLLMR 

       250        260        270        280        290        300 
GIKTLGLRME AIDQNARKIA SFLENHPAVQ TLYYPGSSNH PGHELAKTQG AGFGGMISFD 

       310        320        330        340        350        360 
IGSEERVDAF LGNLKLFTIA ESLGAVESLI SVPARMTHAS IPRERRLELG ITDGLIRISV 

       370 
GIEDAEDLLE DIGQALENI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the Bacillus subtilis genome region in the vicinity of the lev operon reveals two new extracytoplasmic function RNA polymerase sigma factors SigV and SigZ." Sorokin A., Bolotin A., Purnelle B., Hilbert H., Lauber J., Duesterhoeft A., Ehrlich S.D. Microbiology 143:2939-2943(1997) [PubMed: 9308178] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"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. Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Conversion of methionine to cysteine in Bacillus subtilis and its regulation." Hullo M.-F., Auger S., Soutourina O., Barzu O., Yvon M., Danchin A., Martin-Verstraete I. J. Bacteriol. 189:187-197(2007) [PubMed: 17056751] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, DISRUPTION PHENOTYPE. Strain: 168.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U93874 Genomic DNA. Translation: AAB80859.1. AL009126 Genomic DNA. Translation: CAB14667.1.
PIR	A69974.
RefSeq	NP_390603.1. NC_000964.3.
3D structure databases
HSSP	HSSP built from PDB template 1N8P based on UniProtKB P31373.
ProteinModelPortal	O05394.
SMR	O05394. Positions 1-376.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000003482; EBBACP00000003482; EBBACG00000003475.
GeneID	936947.
GenomeReviews	Gene locus BSU27250 in contig AL009126_GR.
KEGG	bsu:BSU27250.
NMPDR	fig\|224308.1.peg.2728.
PATRIC	18977306. VBIBacSub10457_2842.
Organism-specific databases
GenoList	BSU27250. [Micado]
Phylogenomic databases
GeneTree	EBGT00070000031827.
HOGENOM	HBG754729.
OMA	HEHYALA.
PhylomeDB	O05394.
ProtClustDB	PRK07671.
Enzyme and pathway databases
BioCyc	BSUB:BSU27250-MONOMER.
Family and domain databases
InterPro	IPR000277. Cys/Met-Metab_PyrdxlP-dep_enz. 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	K01760.
PANTHER	PTHR11808. Cys_Met_Meta_PP. 1 hit.
Pfam	PF01053. Cys_Met_Meta_PP. 1 hit. [Graphical view]
PIRSF	PIRSF001434. CGS. 1 hit.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITE	PS00868. CYS_MET_METAB_PP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MCCB_BACSU

Accession

Primary (citable) accession number: O05394
Secondary accession number(s): Q795Y3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents