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P50245 (SAHH2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative adenosylhomocysteinase 2
Short name=AdoHcyase 2
EC=3.3.1.1
Alternative name(s):
S-adenosyl-L-homocysteine hydrolase 2
Gene names
Name:Ahcy89E
Synonyms:pH200
ORF Names:CG8956
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.

Cofactor

Binds 1 NAD per subunit By similarity.

Pathway

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

Tissue specificity

Expressed in extended germ band embryos and in somatic mesoderm, yolk cells and midgut during later embryonic stages.

Sequence similarities

Belongs to the adenosylhomocysteinase family.

Sequence caution

The sequence AAA84400.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   LigandNAD
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionadenosylhomocysteinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Putative adenosylhomocysteinase 2
PRO_0000116914

Regions

Nucleotide binding218 – 2203NAD By similarity
Nucleotide binding283 – 2886NAD By similarity
Nucleotide binding360 – 3623NAD By similarity

Sites

Binding site1921Substrate By similarity
Binding site2171Substrate By similarity
Binding site2471Substrate By similarity
Binding site2511Substrate By similarity
Binding site3041NAD By similarity
Binding site3391NAD By similarity
Binding site4071NAD By similarity

Experimental info

Sequence conflict1271T → A in CAA31566. Ref.1
Sequence conflict484 – 4929PFKANYYRY → LLKPITTGWLPFFPFQFCTL VNNILISFADINQYLMLYPV ILVL in CAA31566. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P50245 [UniParc].

Last modified May 30, 2003. Version 2.
Checksum: F4916A43A2A3B288

FASTA49254,241
        10         20         30         40         50         60 
MAKMPETTFA DLSLADKTAV KKSSIEARRF SDVSTCSFSS TCFTGSSDEE DVSPKDNHQR 

        70         80         90        100        110        120 
NSAGGTDFCV KSISKSAFGR REIEIAESEM PGIMTLRKRA KDEKPLKGAN IVGCTHVNAQ 

       130        140        150        160        170        180 
SAVLIETLVQ LGATVRWAAC NIYSTQNAVA AALAEAGIPI FAWRGETEEE FWWCLDRAIY 

       190        200        210        220        230        240 
SDGWQPNLIL DDGGDATHLM LKKYPDYFKA IRGIVEESVT GVHRLYMLSK GGKLTVPAIN 

       250        260        270        280        290        300 
VNDSVTKNKF DTFYTCRDSI LDSLKRTTDI MFGGKQVVIC GYGDVGKGCA QSLKGQGCIV 

       310        320        330        340        350        360 
YVTEVDPICA LQAAMDGFRV VRLNEVIRTV DVVVTATGNK NVITRDHMNR MKNGCILCNM 

       370        380        390        400        410        420 
GHSCSEIDVN GLHTPELTWE RVRSQVDHIR WPDGRMIILL AEGRLVNLSC STISSFVVSV 

       430        440        450        460        470        480 
ASSTQALALI ELFSAPGRYK SDVYLLPKKM DEYVASLHLA TFDAHLTELT DEQSKFMGLN 

       490 
KAGPFKANYY RY

« Hide

References

« Hide 'large scale' references
[1]"Evidence that the Abdominal-B r element function is conferred by a trans-regulatory homeoprotein."
Delorenzi M., Ali N., Saari G., Henry C., Wilcox M., Bienz M.
EMBO J. 7:3223-3231(1988) [PubMed: 2903049] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Embryo.
[2]"Complete sequence of the bithorax complex of Drosophila."
Martin C.H., Mayeda C.A., Davis C.A., Ericsson C.L., Knafels J.D., Mathog D.R., Celniker S.E., Lewis E.B., Palazzolo M.J.
Proc. Natl. Acad. Sci. U.S.A. 92:8398-8402(1995) [PubMed: 7667301] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Canton-S.
[3]"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.
[4]"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.
Strain: Berkeley.
[5]"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: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X13168 Genomic DNA. Translation: CAA31566.1.
U31961 Genomic DNA. Translation: AAA84400.1. Sequence problems.
AE014297 Genomic DNA. Translation: AAF55367.2.
AY113501 mRNA. Translation: AAM29506.1.
PIRS01302.
RefSeqNP_996221.1. NM_206499.1.
NP_996222.1. NM_206500.1.
UniGeneDm.4866.

3D structure databases

ProteinModelPortalP50245.
SMRP50245. Positions 58-488.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-24031N.
IntActP50245. 1 interaction.
MINTMINT-974811.
STRINGP50245.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0083378; FBpp0082821; FBgn0015011.
GeneID42043.
KEGGdme:Dmel_CG8956.

Organism-specific databases

CTD42043.
FlyBaseFBgn0015011. Ahcy89E.

Phylogenomic databases

eggNOGinNOG07657.
GeneTreeEMGT00050000015433.
InParanoidP50245.
OrthoDBEOG402V7D.
PhylomeDBP50245.

Gene expression databases

ArrayExpressP50245.
BgeeP50245.
GermOnlineCG8956. Drosophila melanogaster.

Family and domain databases

InterProIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
KOK01251.
PANTHERPTHR23420. Ad_hcy_hydrolase. 1 hit.
PfamPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
TIGRFAMsTIGR00936. AhcY. 1 hit.
PROSITEPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio826882.

Entry information

Entry nameSAHH2_DROME
AccessionPrimary (citable) accession number: P50245
Secondary accession number(s): Q27587, Q8MYX7, Q9VEQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2003
Last modified: January 25, 2012
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents