Reviewed, UniProtKB/Swiss-Prot O94350 (CBL_SCHPO)

Names and origin

Protein names

Recommended name:
    Cystathionine beta-lyase
      Short name=CBL
    EC=4.4.1.8
Alternative name(s):
    Beta-cystathionase
    Cysteine lyase

Gene names

Name:	str3
ORF Names:	SPCC11E10.01, SPCC61.06

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the trans-sulfuration enzymes family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	methionine biosynthetic process from L-homoserine via cystathionine Inferred by curator. Source: GeneDB_SPombe
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cystathionine beta-lyase 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 – 390	390	Cystathionine beta-lyase		PRO_0000352810
Amino acid modifications
	Modified residue	202	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O94350-1 [UniParc]. Last modified August 21, 2007. Version 4. Checksum: FBC40B8CF2D1CD60	FASTA	390	42,773
	10 20 30 40 50 60 MPSDCKYSVD TELVHVEGNE DQYHASSVPI YQSATFKQPC LEHMGKFDYT RSGNPTRSVL 70 80 90 100 110 120 QVHLAKLMKA KHAFVTSNGM SALDMILRCC KSNSHVVAGH DLYGGSDRLL SFNQRQYGFK 130 140 150 160 170 180 VDNVDTSDLA AFEAALRPDT NLVLIESPTN PRISICDIRA IVKITRSKAK DALLVMDNTM 190 200 210 220 230 240 LSPVLCNPLD FGYDIVYESA TKYLSGHHDL MGGVIATKSD EIAKSVFFNI NAMGAAMAPF 250 260 270 280 290 300 ECFLLLRGIK TMGLRVERAQ QNAIEIAKFL KSKGLQVNFP GLDPDAKSTA IFYSFARGPG 310 320 330 340 350 360 AVMSVFTGDV EVSKTIVNTT KLFEISVSFG AVNSLISMPA YMSHASIKKE VRDARGLSED 370 380 390 LIRICVGIEN VDDLKADLEN ALAQANFKQN

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329672 Genomic DNA. Translation: CAA22275.2.
RefSeq	NP_588197.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O94350.
Genome annotation databases
GeneID	2539019.
GenomeReviews	Gene locus str3 in contig CU329672_GR.
KEGG	spo:SPCC11E10.01.
Organism-specific databases
GeneDB_Spombe	SPCC11E10.01.
Gene expression databases
ArrayExpress	O94350.
Family and domain databases
InterPro	IPR000277. Cys/Met-Metab_PyrdxlP-dep_enz. IPR006238. Cys_b_lyase_euk. 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.
PANTHER	PTHR11808. Cys_Met_Meta_PP. 1 hit.
Pfam	PF01053. Cys_Met_Meta_PP. 1 hit. [Graphical view]
PIRSF	PIRSF001434. CGS. 1 hit.
TIGRFAMs	TIGR01329. cysta_beta_ly_E. 1 hit.
PROSITE	PS00868. CYS_MET_METAB_PP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CBL_SCHPO

Accession

Primary (citable) accession number: O94350

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 4, 2008
Last sequence update:	August 21, 2007
Last modified:	September 22, 2009
This is version 46 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)