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Protein

Cystathionine beta-synthase

Gene

Cbs

Organism
Drosophila melanogaster (Fruit fly)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-serine + L-homocysteine = L-cystathionine + H2O.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi22 – 221Iron (heme axial ligand)Combined sources
Metal bindingi34 – 341Iron (heme axial ligand); via tele nitrogenCombined sources

GO - Molecular functioni

GO - Biological processi

  • cysteine biosynthetic process from serine Source: InterPro
  • cysteine biosynthetic process via cystathionine Source: InterPro
  • determination of adult lifespan Source: FlyBase
  • response to endoplasmic reticulum stress Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationImported

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesisUniRule annotation

Keywords - Ligandi

HemeCombined sources, Iron, Metal-binding, Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

BRENDAi4.2.1.22. 1994.
ReactomeiR-DME-1614603. Cysteine formation from homocysteine.

Names & Taxonomyi

Protein namesi
Recommended name:
Cystathionine beta-synthaseUniRule annotation (EC:4.2.1.22UniRule annotation)
Gene namesi
Name:CbsImported
ORF Names:CG1753Imported, Dmel_CG1753Imported
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0031148. Cbs.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881N6-(pyridoxal phosphate)lysineCombined sources

Interactioni

Protein-protein interaction databases

DIPiDIP-59487N.
MINTiMINT-938597.
STRINGi7227.FBpp0076937.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PC2X-ray1.80A1-522[»]
3PC3X-ray1.55A1-522[»]
3PC4X-ray1.70A1-522[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini385 – 44561CBSInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cysteine synthase/cystathionine beta-synthase family.UniRule annotation
Contains 1 CBS domain.UniRule annotation

Keywords - Domaini

CBS domainUniRule annotation

Phylogenomic databases

eggNOGiKOG1252. Eukaryota.
COG0031. LUCA.
GeneTreeiENSGT00510000047027.
KOiK01697.
OMAiPYANPNN.
OrthoDBiEOG7J70F1.

Family and domain databases

InterProiIPR000644. CBS_dom.
IPR005857. Cysta_beta_synth.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00571. CBS. 1 hit.
PF00291. PALP. 1 hit.
[Graphical view]
SMARTiSM00116. CBS. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01137. cysta_beta. 1 hit.
PROSITEiPS51371. CBS. 1 hit.
PS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VRD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPQPKPYERP ADFIDPGKPS KCKWHLGTAE KSPHIHRGIA HRQQITPNIL
60 70 80 90 100
EVIGCTPLVK LNNIPASDGI ECEMYAKCEF LNPGGSVKDR IGYRMVQDAE
110 120 130 140 150
EQGLLKPGYT IIEPTSGNTG IGLAMACAVK GYKCIIVMPE KMSNEKVSAL
160 170 180 190 200
RTLGAKIIRT PTEAAYDSPE GLIYVAQQLQ RETPNSIVLD QYRNAGNPLA
210 220 230 240 250
HYDGTAAEIL WQLDNKVDMI VVSAGTAGTI SGIGRKIKEQ VPSCQIVGVD
260 270 280 290 300
PYGSILARPA ELNKTDVQFY EVEGIGYDFP PTVFDDTVVD VWTKIGDSDC
310 320 330 340 350
FPMSRRLNAE EGLLCGGSSG GAMHAALEHA RKLKKGQRCV VILPDGIRNY
360 370 380 390 400
MTKFVSDNWM EARNFKEPVN EHGHWWWSLA IAELELPAPP VILKSDATVG
410 420 430 440 450
EAIALMKKHR VDQLPVVDQD DGSVLGVVGQ ETLITQIVSM NRQQSDPAIK
460 470 480 490 500
ALNKRVIRLN ESEILGKLAR VLEVDPSVLI LGKNPAGKVE LKALATKLDV
510 520
TTFIAAGKQK PKANGTTNGG SH
Length:522
Mass (Da):56,882
Last modified:May 1, 2000 - v1
Checksum:i880D12F37E9D7CC9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF50862.1.
AE014298 Genomic DNA. Translation: AAF50863.1.
AY058508 mRNA. Translation: AAL13737.1.
AE014298 Genomic DNA. Translation: AHN59978.1.
RefSeqiNP_001285508.1. NM_001298579.1.
NP_608424.1. NM_134580.3.
NP_728384.1. NM_167726.2.
UniGeneiDm.4181.

Genome annotation databases

EnsemblMetazoaiFBtr0077244; FBpp0076937; FBgn0031148.
FBtr0077245; FBpp0076938; FBgn0031148.
FBtr0340437; FBpp0309380; FBgn0031148.
GeneIDi33081.
KEGGidme:Dmel_CG1753.
UCSCiCG1753-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF50862.1.
AE014298 Genomic DNA. Translation: AAF50863.1.
AY058508 mRNA. Translation: AAL13737.1.
AE014298 Genomic DNA. Translation: AHN59978.1.
RefSeqiNP_001285508.1. NM_001298579.1.
NP_608424.1. NM_134580.3.
NP_728384.1. NM_167726.2.
UniGeneiDm.4181.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PC2X-ray1.80A1-522[»]
3PC3X-ray1.55A1-522[»]
3PC4X-ray1.70A1-522[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59487N.
MINTiMINT-938597.
STRINGi7227.FBpp0076937.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077244; FBpp0076937; FBgn0031148.
FBtr0077245; FBpp0076938; FBgn0031148.
FBtr0340437; FBpp0309380; FBgn0031148.
GeneIDi33081.
KEGGidme:Dmel_CG1753.
UCSCiCG1753-RA. d. melanogaster.

Organism-specific databases

CTDi875.
FlyBaseiFBgn0031148. Cbs.

Phylogenomic databases

eggNOGiKOG1252. Eukaryota.
COG0031. LUCA.
GeneTreeiENSGT00510000047027.
KOiK01697.
OMAiPYANPNN.
OrthoDBiEOG7J70F1.

Enzyme and pathway databases

BRENDAi4.2.1.22. 1994.
ReactomeiR-DME-1614603. Cysteine formation from homocysteine.

Miscellaneous databases

GenomeRNAii33081.
NextBioi781844.

Family and domain databases

InterProiIPR000644. CBS_dom.
IPR005857. Cysta_beta_synth.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00571. CBS. 1 hit.
PF00291. PALP. 1 hit.
[Graphical view]
SMARTiSM00116. CBS. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01137. cysta_beta. 1 hit.
PROSITEiPS51371. CBS. 1 hit.
PS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  2. Hwang S.Y., Kim S.E., Biro S., Choi Y.C.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BerkeleyImported.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BerkeleyImported.
  5. "The transposable elements of the Drosophila melanogaster euchromatin: a genomics perspective."
    Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., Celniker S.E.
    Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  6. "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."
    Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., Karpen G.H.
    Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  7. "Combined evidence annotation of transposable elements in genome sequences."
    Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., Ashburner M., Anxolabehere D.
    PLoS Comput. Biol. 1:166-175(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  8. "Drosophila melanogaster release 4 sequence."
    Berkeley Drosophila Genome Project
    Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C., Rubin G.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  9. O'Boyle S.T.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  10. "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."
    Smith C.D., Shu S., Mungall C.J., Karpen G.H.
    Science 316:1586-1591(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  12. "Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine {beta}-synthase."
    Koutmos M., Kabil O., Smith J.L., Banerjee R.
    Proc. Natl. Acad. Sci. U.S.A. 107:20958-20963(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH HEME, PYRIDOXAL PHOSPHATE AT LYS-88.
  13. Millard Andrew
    Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiQ9VRD9_DROME
AccessioniPrimary (citable) accession number: Q9VRD9
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.