Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q27580 (SAHH_DROME)

Last modified November 4, 2008. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Adenosylhomocysteinase
      Short name=AdoHcyase
    EC=3.3.1.1
Alternative name(s):
    S-adenosyl-L-homocysteine hydrolase
Gene names
Name: Ahcy13
Synonyms: ahcY
ORF Names: CG11654
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Hide | Top

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methinine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.

Catalytic activity

S-adenosyl-L-homocysteine + H(2)O = L-homocysteine + adenosine.

Cofactor

Binds 1 NAD per subunit By similarity.

Pathway

Amino-acid biosynthesis; homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.

Sequence similarities

Belongs to the adenosylhomocysteinase family.

Hide | Top

Ontologies

Keywords

   Biological processOne-carbon metabolism
   LigandNAD
   Molecular functionHydrolase
   Technical termComplete proteome

Gene Ontology (GO)

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9VWD61EBI-171029,EBI-161741
WQ241061EBI-171029,EBI-135509

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Adenosylhomocysteinase
PRO_0000116913

Regions

Region183 – 350168NAD binding By similarity

Sites

Binding site561Substrate By similarity
Binding site1311Substrate By similarity
Binding site1561Substrate By similarity
Binding site1861Substrate By similarity
Binding site1901Substrate By similarity

Experimental info

Sequence conflict1461Y → F in CAA64892. Ref.1
Sequence conflict2651A → G in CAA64892. Ref.1
Sequence conflict2941A → R in CAA64892. Ref.1
Sequence conflict326 – 3283DRY → IRH in AAM27497. Ref.4
Sequence conflict3311Q → K in CAA64892. Ref.1
Sequence conflict3511H → D in CAA64892. Ref.1
Sequence conflict379 – 3802YA → S in CAA64892. Ref.1

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q27580-1 [UniParc].

Last modified October 25, 2005. Version 2.
Checksum: 2977DAF12B40C324

FASTA43247,366
        10         20         30         40         50         60 
MSKPSYKVAD ISLAEWGRKA IIIAENEMPG LMACRKKYGP SKPLKGARIT GCLHMTVQTA 

        70         80         90        100        110        120 
VLIETLVELG AQVQWSSCNI FSTQDNAAAA IAATGVPVYA WKGETDEEYM WCIEQTLVFP 

       130        140        150        160        170        180 
DGQPLNMILD DGGDLTNLVH EKFPQYLKNI KGLSEETTTG VHNLYKMFKE GRLGVPAINV 

       190        200        210        220        230        240 
NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVCCVAG YGDVGKGCAQ ALKGFGGRVI 

       250        260        270        280        290        300 
VTEVDPINAL QAAMEGYEVT TMEEASKEAS IFVTTTGCRD IITSVHLQQM PDDAIVCNIG 

       310        320        330        340        350        360 
HFDIEIDVDW LNANAKEKVN VKPQVDRYTM QSGKHIILLA EGRLVNLGCA HGHPSFVMSN 

       370        380        390        400        410        420 
SFTNQVLAQI ELWTKSDKYA VGVHVLPKIL DEEVASLHLE KLGVKLTKLT EKQATYLGVS 

       430 
QTGPFKPDHY RY

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"The S-adenosyl-L-homocysteine hydrolase of Drosophila melanogaster: identification, deduced amino acid sequence and cytological localization of the structural gene."
Caggese C., Ragone G., Barsanti P., Moschetti R., Messina A., Massari S., Caizzi R.
Mol. Gen. Genet. 253:492-498(1997) [PubMed: 9037110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., 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.A., 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.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., 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.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., 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., Woodage T., 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.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Ovary.

Hide | Top

Cross-references

Sequence databases

X95636 mRNA. Translation: CAA64892.1.
AE014298 Genomic DNA. Translation: AAF48453.1.
AY102668 mRNA. Translation: AAM27497.1.
RefSeqNP_511164.2.
UniGeneDm.7858

3D structure databases

HSSPHSSP built from PDB template 1LI4 based on UniProtKB P23526.
SMRQ27580. Positions 3-432.
ModBaseSearch...

Protein-protein interaction databases

IntActQ27580.

Genome annotation databases

EnsemblCG11654. Drosophila melanogaster. [Contig view]
GeneID32471.
KEGGdme:Dmel_CG11654.
NMPDRfig|7227.3.peg.17936.

Organism-specific databases

FlyBaseFBgn0014455. Ahcy13.

Phylogenomic databases

HOGENOMQ27580.

Gene expression databases

ArrayExpressQ27580.
GermOnlineCG11654. Drosophila melanogaster.

Family and domain databases

InterProIPR000043. Ad_hcy_hydrolase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.1480. Ad_hcy_hydrolase. 1 hit.
PANTHERPTHR23420. Ad_hcy_hydrolase. 1 hit.
PfamPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFPIRSF001109. Ad_hcy_hydrolase. 1 hit.
TIGRFAMsTIGR00936. ahcY. 1 hit.
PROSITEPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

NextBio778633.

Hide | Top

Entry information

Entry nameSAHH_DROME
AccessionPrimary (citable) accession number: Q27580
Secondary accession number(s): Q8MZI1, Q9VXV5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 25, 2005
Last modified: November 4, 2008
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Hide | Top

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents