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Protein

Adenosylhomocysteinase

Gene

ahcy

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

NAD+UniRule annotationNote: Binds 1 NAD+ per subunit.UniRule annotation

Pathwayi: L-homocysteine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-homocysteine from S-adenosyl-L-homocysteine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Adenosylhomocysteinase (ahcyl1), Adenosylhomocysteinase (zgc:158222), Adenosylhomocysteinase (ahcyl1), Adenosylhomocysteinase (ahcyl1), Adenosylhomocysteinase (ahcyl1), Adenosylhomocysteinase (ahcyl2), Adenosylhomocysteinase (zgc:158222), Adenosylhomocysteinase (ahcyl1), Adenosylhomocysteinase (ahcyl1), Adenosylhomocysteinase (ahcy)
This subpathway is part of the pathway L-homocysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homocysteine from S-adenosyl-L-homocysteine, the pathway L-homocysteine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571SubstrateUniRule annotation
Binding sitei132 – 1321SubstrateUniRule annotation
Binding sitei157 – 1571SubstrateUniRule annotation
Binding sitei187 – 1871SubstrateUniRule annotation
Binding sitei191 – 1911SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

  • one-carbon metabolic process Source: UniProtKB-KW
  • S-adenosylmethionine cycle Source: ZFIN
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotationImported

Keywords - Biological processi

One-carbon metabolismUniRule annotation

Keywords - Ligandi

NADUniRule annotation

Enzyme and pathway databases

BRENDAi3.3.1.1. 928.
ReactomeiR-DRE-156581. Methylation.
R-DRE-1614635. Sulfur amino acid metabolism.
UniPathwayiUPA00314; UER00076.

Names & Taxonomyi

Protein namesi
Recommended name:
AdenosylhomocysteinaseUniRule annotation (EC:3.3.1.1UniRule annotation)
Gene namesi
Name:ahcyImported
Synonyms:AHCYImported
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)Imported
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 6

Organism-specific databases

ZFINiZDB-GENE-031219-6. ahcy.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000002844.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini192 – 353162AdoHcyase_NADInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adenosylhomocysteinase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG1370. Eukaryota.
COG0499. LUCA.
GeneTreeiENSGT00390000003626.
HOGENOMiHOG000227987.
HOVERGENiHBG005041.
KOiK01251.
OMAiVHDKYPQ.
OrthoDBiEOG76739S.
TreeFamiTF300415.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00563. AdoHcyase.
InterProiIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERiPTHR23420. PTHR23420. 1 hit.
PfamiPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTiSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00936. ahcY. 1 hit.
PROSITEiPS00738. ADOHCYASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q803T5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKLPFKVA DISLAEWGRK AIEIAENEMP GLMKMRELYG QSKPLKGARI
60 70 80 90 100
AGCLHMTLQT AVLIETLTAL GAEVQWSSCN IFSTQDHAAA AIAKTGVPVY
110 120 130 140 150
AWKGETDEEY VWCIEQTIYF KDGQPLNMIL DDGGDLTNLV HQKYPKLLAG
160 170 180 190 200
IKGISEETTT GVHNLYKMLK SGELKVPAIN VNDSVTKSKF DNLYGCRESL
210 220 230 240 250
IDGIKRATDV MIAGKVAVVA GYGDVGKGCV QALRGFGARV IVTEIDPINA
260 270 280 290 300
LQAAMEGYEV TTMDEACKEG NIFVTTTGCE DILLGRHFEH MKDDSIVCNI
310 320 330 340 350
GHFDCEIDMK WLNEHAAKKI NIKPQVDRYR MKNGRHIIVL AEGRLVNLGC
360 370 380 390 400
AMGHPSFVMS NSFTNQVLAQ IELWKNNSKY PLGVYFLPKK LDEEVAAAHL
410 420 430
DKLGVKLTKL TEKQAKYLGL PSEGPFKPDH YRY
Length:433
Mass (Da):47,964
Last modified:June 1, 2003 - v1
Checksum:iFC8D6DC796DD0018
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX629346 Genomic DNA. No translation available.
BC044200 mRNA. Translation: AAH44200.1.
BC164526 mRNA. Translation: AAI64526.1.
AY398307 mRNA. Translation: AAQ97740.1.
RefSeqiNP_954688.1. NM_199218.1.
UniGeneiDr.935.

Genome annotation databases

EnsembliENSDART00000018523; ENSDARP00000002844; ENSDARG00000005191.
ENSDART00000159742; ENSDARP00000130781; ENSDARG00000005191.
GeneIDi387530.
KEGGidre:387530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX629346 Genomic DNA. No translation available.
BC044200 mRNA. Translation: AAH44200.1.
BC164526 mRNA. Translation: AAI64526.1.
AY398307 mRNA. Translation: AAQ97740.1.
RefSeqiNP_954688.1. NM_199218.1.
UniGeneiDr.935.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000002844.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000018523; ENSDARP00000002844; ENSDARG00000005191.
ENSDART00000159742; ENSDARP00000130781; ENSDARG00000005191.
GeneIDi387530.
KEGGidre:387530.

Organism-specific databases

CTDi191.
ZFINiZDB-GENE-031219-6. ahcy.

Phylogenomic databases

eggNOGiKOG1370. Eukaryota.
COG0499. LUCA.
GeneTreeiENSGT00390000003626.
HOGENOMiHOG000227987.
HOVERGENiHBG005041.
KOiK01251.
OMAiVHDKYPQ.
OrthoDBiEOG76739S.
TreeFamiTF300415.

Enzyme and pathway databases

UniPathwayiUPA00314; UER00076.
BRENDAi3.3.1.1. 928.
ReactomeiR-DRE-156581. Methylation.
R-DRE-1614635. Sulfur amino acid metabolism.

Miscellaneous databases

NextBioi20814154.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00563. AdoHcyase.
InterProiIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERiPTHR23420. PTHR23420. 1 hit.
PfamiPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTiSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00936. ahcY. 1 hit.
PROSITEiPS00738. ADOHCYASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: ABImported.
    Tissue: Whole bodyImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: Kidney marrowImported.
  3. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: PCR rescueImported.
  4. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: TuebingenImported.
  5. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TuebingenImported.
  6. Ensembl
    Submitted (NOV-2015) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: TuebingenImported.

Entry informationi

Entry nameiQ803T5_DANRE
AccessioniPrimary (citable) accession number: Q803T5
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: May 11, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

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.