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Q3AQC2 (SAHH_CHLCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:Cag_1548
OrganismChlorobium chlorochromatii (strain CaD3) [Complete proteome] [HAMAP]
Taxonomic identifier340177 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobium/Pelodictyon group › Chlorobium

Protein attributes

Sequence length471 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 – 471471Adenosylhomocysteinase HAMAP MF_00563
PRO_1000024722

Regions

Nucleotide binding197 – 1993NAD By similarity
Nucleotide binding260 – 2656NAD By similarity
Nucleotide binding339 – 3413NAD By similarity

Sites

Binding site601Substrate By similarity
Binding site1351Substrate By similarity
Binding site1961Substrate By similarity
Binding site2261Substrate By similarity
Binding site2301Substrate By similarity
Binding site2311NAD By similarity
Binding site2831NAD By similarity
Binding site3181NAD By similarity
Binding site3871NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3AQC2 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 04F2691F7CF61C72

FASTA47152,247
        10         20         30         40         50         60 
MSTVAEALAY KVADISLAEW GRKEIEIAEK EMPGLMALRK KYAGQKPLKG ARIAGSLHMT 

        70         80         90        100        110        120 
IQTAVLIETL VDLGANVRWA SCNIFSTQDH AAAAIAQAGV PVFAWKGETL DEYWWCTRQI 

       130        140        150        160        170        180 
LEFDGGLGPN LIVDDGGDAT LMIILGHKIE NDPKMLDKTP GNAEEKALYQ QLREVFAEDN 

       190        200        210        220        230        240 
QRWHKVAADM KGVSEETTTG VHRLYQMMEK GELLFPAINV NDSVTKSKFD NLYGCRESLA 

       250        260        270        280        290        300 
DGIKRATDVM IAGKVTVVLG YGDVGKGCAH SMRSYGARVI VTEIDPICAL QAAMEGFEVA 

       310        320        330        340        350        360 
TMEDAVHEGN IFVTTTGNKD VITLEHMKQM RDEAIVCNIG HFDNEIQVDK LNNDPTVKII 

       370        380        390        400        410        420 
NIKPQVDKYI FPNGNCMYLL AEGRLVNLGC ATGHPSFVMS NSFTNQTLAQ IELWQKEYAV 

       430        440        450        460        470 
DVYRLPKALD EEVARLHLEQ IGVRLTRLTP EQAEYIGVSA DGPYKPEHYR Y

« Hide

References

[1]"Complete sequence of Chlorobium chlorochromatii CaD3."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CaD3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000108 Genomic DNA. Translation: ABB28803.1.
RefSeqYP_379846.1. NC_007514.1.

3D structure databases

HSSPHSSP built from PDB template 1K0U based on UniProtKB P10760.
ProteinModelPortalQ3AQC2.
SMRQ3AQC2. Positions 10-471.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3AQC2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3746548.
GenomeReviewsGene locus Cag_1548 in contig CP000108_GR.
KEGGcch:Cag_1548.
PATRIC21370815. VBIChlChl46571_1605.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0499.
HOGENOMHBG352029.
OMASAQVWVT.
PhylomeDBQ3AQC2.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycCCHL340177:CAG_1548-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_CHLCH
AccessionPrimary (citable) accession number: Q3AQC2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 52 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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