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Q0ALW1 (SAHH_MARMM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:Mmar10_2440
OrganismMaricaulis maris (strain MCS10) [Complete proteome] [HAMAP]
Taxonomic identifier394221 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Hyphomonadaceae › Maricaulis

Protein attributes

Sequence length469 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 – 469469Adenosylhomocysteinase HAMAP MF_00563
PRO_1000061127

Regions

Nucleotide binding196 – 1983NAD By similarity
Nucleotide binding259 – 2646NAD By similarity
Nucleotide binding338 – 3403NAD By similarity

Sites

Binding site601Substrate By similarity
Binding site1351Substrate By similarity
Binding site1951Substrate By similarity
Binding site2251Substrate By similarity
Binding site2291Substrate By similarity
Binding site2301NAD By similarity
Binding site2821NAD By similarity
Binding site3171NAD By similarity
Binding site3831NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0ALW1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 132FEE516538AE35

FASTA46951,834
        10         20         30         40         50         60 
MTQFAADKPY IVKDMSLAKW GRIEFDMAEI EMPGLMALRE EYKDSQPLKG ARIAGSLHMT 

        70         80         90        100        110        120 
VQTAILIETL TALGAEVRWA SCNIFSTQDH AAAAIAETGV PVFATKGETL EEYWDYADAI 

       130        140        150        160        170        180 
FHWPDGETAN MILDDGGDAT MYLILGEKAE NDPSVLNHPK SEEETFLFAQ IKKRIAATPG 

       190        200        210        220        230        240 
WFAKAKAAIQ GVSEETTTGV MRLYQMQKRG ELPFPAINVN DSVTKSKFDN RYGCRESLVD 

       250        260        270        280        290        300 
AIRRGTDVMM AGKKALVFGY GDVGKGSAES LAGAGARVYV TEIDPICALQ ACMDGFEVVR 

       310        320        330        340        350        360 
AEDVIGEMDI FVTATGNKDI LTVDHMRAMK DMAIVCNIGH FDNEIQVESL KNYQWTNVKP 

       370        380        390        400        410        420 
QVDLVNFPEG HRIILLSEGR LVNLGNATGH PSFVMSASFT NQTLAQIELW TKGENYTNEV 

       430        440        450        460 
YILPKHLDEK VAALHLDKLG AKLTVLSDEQ ADYIGVPQHG PFKAEHYRY

« Hide

References

[1]"Complete sequence of Maricaulis maris MCS10."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., Stephens C., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000449 Genomic DNA. Translation: ABI66732.1.
RefSeqYP_757670.1. NC_008347.1.

3D structure databases

ProteinModelPortalQ0ALW1.
SMRQ0ALW1. Positions 10-469.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0ALW1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4285422.
GenomeReviewsGene locus Mmar10_2440 in contig CP000449_GR.
KEGGmmr:Mmar10_2440.
NMPDRfig|394221.5.peg.2393.
PATRIC22453070. VBIMarMar77530_2503.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0499.
HOGENOMHBG352029.
OMASAQVWVT.
PhylomeDBQ0ALW1.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycMMAR394221:MMAR10_2440-MONOMER.

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_MARMM
AccessionPrimary (citable) accession number: Q0ALW1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 17, 2006
Last modified: January 25, 2012
This is version 47 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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