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Q64MT2 (SAHH_BACFR) 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:BF4468
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length487 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 – 487487Adenosylhomocysteinase HAMAP MF_00563
PRO_0000116942

Regions

Nucleotide binding213 – 2153NAD By similarity
Nucleotide binding276 – 2816NAD By similarity
Nucleotide binding355 – 3573NAD By similarity

Sites

Binding site761Substrate By similarity
Binding site1511Substrate By similarity
Binding site2121Substrate By similarity
Binding site2421Substrate By similarity
Binding site2461Substrate By similarity
Binding site2471NAD By similarity
Binding site2991NAD By similarity
Binding site3341NAD By similarity
Binding site4031NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64MT2 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 64AA176C52CF0B00

FASTA48754,186
        10         20         30         40         50         60 
MFYLCTTLYF KQFTFMSTEL FSTLPYKVAD ITLADFGRKE IDLAEKEMPG LMALREKYGE 

        70         80         90        100        110        120 
SKPLKGARIM GSLHMTIQTA VLIETLVALG AEVRWCSCNI YSTQDHAAAA IAASGVAVFA 

       130        140        150        160        170        180 
WKGETLADYW WCTLQALNFE GGKGPTVIVD DGGDATMMIH VGYEAENNAA VLDKEVHAED 

       190        200        210        220        230        240 
EIELNAILKK VLAEDKERWH RVAAEVRGVS EETTTGVHRL YQMQEEGKLL FPAFNVNDSV 

       250        260        270        280        290        300 
TKSKFDNLYG CRESLADGIK RATDVMIAGK VVVVCGYGDV GKGCSHSMRS YGARVLVTEV 

       310        320        330        340        350        360 
DPICALQAAM EGFEVVTMED ACKEGNIFVT TTGNIDIIRI DHMEQMKDQA IVCNIGHFDN 

       370        380        390        400        410        420 
EIQVDALKHY PGIKRVNIKP QVDRYYFPDG HSIILLADGR LVNLGCATGH PSFVMSNSFT 

       430        440        450        460        470        480 
NQTLAQIELF NKKYDINVYR LPKHLDEEVA RLHLEKIGVK LTKLTPEQAA YIGVSVDGPY 


KADHYRY

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP006841 Genomic DNA. Translation: BAD51205.1.
RefSeqYP_101739.1. NC_006347.1.

3D structure databases

ProteinModelPortalQ64MT2.
SMRQ64MT2. Positions 26-487.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3085544.
GenomeReviewsGene locus BF4468 in contig AP006841_GR.
KEGGbfr:BF4468.
PATRIC21054513. VBIBacFra17906_4306.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG352029.
OMASAQVWVT.
ProtClustDBPRK05476.

Enzyme and pathway databases

BioCycBFRA295405:BF4468-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_BACFR
AccessionPrimary (citable) accession number: Q64MT2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 51 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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