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Q2SLT4 (SAHH_HAHCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:HCH_01532
OrganismHahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]
Taxonomic identifier349521 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Hahellaceae › Hahella

Protein attributes

Sequence length463 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 – 463463Adenosylhomocysteinase HAMAP MF_00563
PRO_1000024728

Regions

Nucleotide binding165 – 1673NAD By similarity
Nucleotide binding228 – 2336NAD By similarity
Nucleotide binding321 – 3233NAD By similarity

Sites

Binding site631Substrate By similarity
Binding site1391Substrate By similarity
Binding site1641Substrate By similarity
Binding site1941Substrate By similarity
Binding site1981Substrate By similarity
Binding site1991NAD By similarity
Binding site2511NAD By similarity
Binding site3001NAD By similarity
Binding site3691NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2SLT4 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 40D703C8EAE28FF6

FASTA46351,348
        10         20         30         40         50         60 
MAQLQSVDNF SDYKVKDISL AAWGRKEIDI AEGEMPALMT LREKYRAQQP LAGARILGCI 

        70         80         90        100        110        120 
HMTIQTAVLI ETLVALGAEV RWSSCNIFST QDHAAAAIAA AGVPVFAWKG ETEEEYVWCI 

       130        140        150        160        170        180 
KQTITKDGQP WNANMVLDDG GDLTEILHNE FPQMLDHIHG ISEETTTGVH RLLDMMKKGE 

       190        200        210        220        230        240 
LKVPAVNVND SVTKSKNDNK YGCRHSLNDA IKRATDHLLA GKKALVIGYG DVGKGSAASL 

       250        260        270        280        290        300 
RQEGMIVKIS EIDPICAMQA CMDGYEVVSP YIDGVNTGAA DGVNRDLLGH TDLLVTTTGN 

       310        320        330        340        350        360 
VNVCDKYMLQ ALKSGAVVCN IGHFDNEIDT RFMRDNWEWE EVKPQVHVIY RNKDQNDHLL 

       370        380        390        400        410        420 
LLSEGRLVNL GNATGHPSRI MDGSFANQVL AQMYLFERKF ADLPADEKPK NLYVRVLPKQ 

       430        440        450        460 
LDEEVARYMV QGFGGVITKL TQPQAKYIGV EVEGPYKPTD YKY

« Hide

References

[1]"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent."
Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F.
Nucleic Acids Res. 33:7066-7073(2005) [PubMed: 16352867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KCTC 2396.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000155 Genomic DNA. Translation: ABC28390.1.
RefSeqYP_432815.1. NC_007645.1.

3D structure databases

HSSPHSSP built from PDB template 1K0U based on UniProtKB P10760.
ProteinModelPortalQ2SLT4.
SMRQ2SLT4. Positions 10-463.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2SLT4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3837562.
GenomeReviewsGene locus HCH_01532 in contig CP000155_GR.
KEGGhch:HCH_01532.
NMPDRfig|349521.5.peg.1378.
PATRIC22084022. VBIHahChe29232_1417.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0499.
HOGENOMHBG352029.
OMASAQVWVT.
PhylomeDBQ2SLT4.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycHCHE349521:HCH_01532-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_HAHCH
AccessionPrimary (citable) accession number: Q2SLT4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 50 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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