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A9C184 (SAHH_DELAS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenosylhomocysteinase
EC=3.3.1.1
Alternative name(s):
S-adenosyl-L-homocysteine hydrolase
Short name=AdoHcyase
Gene names
Name:ahcY
Ordered Locus Names:Daci_5919
OrganismDelftia acidovorans (strain DSM 14801 / SPH-1) [Complete proteome] [HAMAP]
Taxonomic identifier398578 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Delftia

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine By similarity. HAMAP MF_00563

Catalytic activity

S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine. HAMAP MF_00563

Cofactor

Binds 1 NAD per subunit By similarity. HAMAP MF_00563

Pathway

Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. HAMAP MF_00563

Subcellular location

Cytoplasm By similarity HAMAP MF_00563.

Sequence similarities

Belongs to the adenosylhomocysteinase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionadenosylhomocysteinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476Adenosylhomocysteinase HAMAP MF_00563
PRO_1000129282

Regions

Nucleotide binding202 – 2043NAD By similarity
Nucleotide binding265 – 2706NAD By similarity
Nucleotide binding344 – 3463NAD By similarity

Sites

Binding site621Substrate By similarity
Binding site1411Substrate By similarity
Binding site2011Substrate By similarity
Binding site2311Substrate By similarity
Binding site2351Substrate By similarity
Binding site2361NAD By similarity
Binding site2881NAD By similarity
Binding site3231NAD By similarity
Binding site3891NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A9C184 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: D509C3789698C0EB

FASTA47651,762
        10         20         30         40         50         60 
MNAAVRPVSA DTAIADISLA AWGRKEILIA ETEMPGLMAT REEFAAAQPL KGARIAGSLH 

        70         80         90        100        110        120 
MTIQTAVLIE TLKALGAEVR WASCNIFSTQ DHAAAAIAET GTPVFAIKGE SLADYWDYTH 

       130        140        150        160        170        180 
RIFEFGAAGT EGEGPNMILD DGGDATMLLH LGMRAEKDLS VLDNPASEEE KIAFAAIRAK 

       190        200        210        220        230        240 
LAQDPTWYTR KSAHIIGVTE ETTTGVHRLN EMSAKGTLKF RAINVNDSVT KSKFDNLYGC 

       250        260        270        280        290        300 
RESLVDGIKR ATDVMIAGKV AVVAGYGDVG KGCAQALRAL SAQVWVTEID PINALQAAME 

       310        320        330        340        350        360 
GYKVVTMEWA ADKADIFVTT TGNRDIIRHE HMVAMKNEAI VCNIGHFDNE IDVASIEQYQ 

       370        380        390        400        410        420 
WEEIKPQVDH ITFPDGKKII LLAKGRLVNL GCATGHPSFV MSASFANQTI AQIELFTKPD 

       430        440        450        460        470 
AYEVGKVYVL PKILDEKVAR LHLKKVGAML TELTDGQAAY IGVSKQGPYK PETYRY

« Hide

References

[1]"Complete sequence of Delftia acidovorans DSM 14801 / SPH-1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14801 / SPH-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000884 Genomic DNA. Translation: ABX38547.1.
RefSeqYP_001566932.1. NC_010002.1.

3D structure databases

ProteinModelPortalA9C184.
SMRA9C184. Positions 11-476.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9C184.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5751540.
GenomeReviewsGene locus Daci_5919 in contig CP000884_GR.
KEGGdac:Daci_5919.
PATRIC21645925. VBIDelAci41351_5987.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG352029.
OMASAQVWVT.
ProtClustDBPRK05476.

Family and domain databases

HAMAPMF_00563. AdoHcyase.
[Tree]
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...

Entry information

Entry nameSAHH_DELAS
AccessionPrimary (citable) accession number: A9C184
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 15, 2008
Last modified: January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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