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Q6MNC0 (SAHH_BDEBA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. 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:Bd1339
OrganismBdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) [Complete proteome] [HAMAP]
Taxonomic identifier264462 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Bdellovibrionales › Bdellovibrionaceae › Bdellovibrio

Protein attributes

Sequence length460 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.

Sequence caution

The sequence CAE79232.1 differs from that shown. Reason: Erroneous initiation.

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 – 460460Adenosylhomocysteinase HAMAP MF_00563
PRO_0000116946

Regions

Nucleotide binding185 – 1873NAD By similarity
Nucleotide binding248 – 2536NAD By similarity
Nucleotide binding327 – 3293NAD By similarity

Sites

Binding site831Substrate By similarity
Binding site1581Substrate By similarity
Binding site1841Substrate By similarity
Binding site2141Substrate By similarity
Binding site2181Substrate By similarity
Binding site2191NAD By similarity
Binding site2711NAD By similarity
Binding site3731NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MNC0 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: 36EC82E3C8242381

FASTA46050,853
        10         20         30         40         50         60 
MKKNAKMKAP TATKTAAKTP VVDYRVSKEA MENPEVFAKL AKWGREEIKI AETEMPGLMA 

        70         80         90        100        110        120 
LRKEYKKQQP LKGARIAGCL HMTIQTAVLI ETLVELGAEI RWSSCNIFST QDHAAAAIAA 

       130        140        150        160        170        180 
AGIPVFAWKG LTEQEFNWCI EQTIVGWGKE GFNMILDDGG DLTNMMHEPR FAKEMKKIIG 

       190        200        210        220        230        240 
ISEETTTGVH NLEVLVKQGK LKVPAININD SVTKSKFDNL YGCRESLADG IKRATDVMVA 

       250        260        270        280        290        300 
GKICVVAGYG DVGKGSAHSL RGLGARVLVT EIDPICALQA AMEGFEVTTM EDAAPLGDIF 

       310        320        330        340        350        360 
VTATGCCDII TDKHFMKMKN NAIVCNIGHF DIEIDMAWLN KNSKMREVKP QVDIHTLKNG 

       370        380        390        400        410        420 
KQVIILAKGR LVNLGCATGH PSFVMSNSFT NQVLAQMELF NNRDKYQDIA VYRLPKHLDE 

       430        440        450        460 
KVAALHLDKL GVKLTKLSSK QAKYLHMSPQ GPFKPEHYRY

« Hide

References

[1]"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
Science 303:689-692(2004) [PubMed: 14752164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15356 / DSM 50701 / NCIB 9529 / HD100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842649 Genomic DNA. Translation: CAE79232.1. Different initiation.

3D structure databases

ProteinModelPortalQ6MNC0.
SMRQ6MNC0. Positions 40-460.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GenomeReviewsGene locus Bd1339 in contig BX842601_GR.
KEGGbba:Bd1339.
NMPDRfig|264462.1.peg.1209.
PATRIC21077266. VBIBdeBac73187_1213.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG352029.
PhylomeDBQ6MNC0.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycBBAC264462:BD1339-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_BDEBA
AccessionPrimary (citable) accession number: Q6MNC0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: January 25, 2012
This is version 51 of the entry and version 2 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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