ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8A407


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name SAHH_BACTN
Primary accession number Q8A407
Secondary accession numbers None
Integrated into Swiss-Prot on June 20, 2003
Sequence was last modified on June 20, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 42)
Name and origin of the protein
Protein name Adenosylhomocysteinase
Synonyms EC 3.3.1.1
S-adenosyl-L-homocysteine hydrolase
AdoHcyase
Gene name
Name: ahcY
OrderedLocusNames: BT_2797
From
Bacteroides thetaiotaomicron [TaxID: 818] [HAMAP proteome]
Taxonomy Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
DOI=10.1126/science.1080029; PubMed=12663928 [NCBI, ExPASy, EBI, Israel, Japan]
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.;
"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
Science 299:2074-2076(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE015928; AAO77903.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_811709.1; -.
3D structure databases
HSSP P23526; 1LI4. [HSSP ENTRY / PDB]
ModBase Q8A407.
Enzyme and pathway databases
BioCyc BTHE226186:BT_2797-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004013; Molecular function: adenosylhomocysteinase activity (inferred from electronic annotation from HAMAP).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00563; -; 1.
PBIL [Tree]
InterPro IPR000043; Ad_hcy_hydrolase.
IPR015878; Ado_hCys_hydrolase_NAD-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.1480; Ad_hcy_hydrolase; 1.
PANTHER PTHR23420; Ad_hcy_hydrolase; 1.
Pfam PF05221; AdoHcyase; 1.
PF00670; AdoHcyase_NAD; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001109; Ad_hcy_hydrolase; 1.
TIGRFAMs TIGR00936; ahcY; 1.
PROSITE PS00738; ADOHCYASE_1; 1.
PS00739; ADOHCYASE_2; 1.
BLOCKS Q8A407.
ProtoNet Q8A407.
Genome annotation databases
GeneID 1072485; -.
GenomeReviews AE015928_GR; BT_2797.
KEGG bth:BT_2797; -.
NMPDR fig|226186.1.peg.2796; -.
Phylogenomic databases
HOGENOM Q8A407; -.
Genome annotation databases
CMR Q8A407; BT_2797.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Hydrolase; NAD; One-carbon metabolism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   476  476     Adenosylhomocysteinase. PRO_0000116943
REGION   228   396  169     NAD binding (By similarity). 
BINDING   65    65        Substrate (By similarity). 
BINDING   140   140        Substrate (By similarity). 
BINDING   201   201        Substrate (By similarity). 
BINDING   231   231        Substrate (By similarity). 
BINDING   235   235        Substrate (By similarity). 
Sequence information
Length: 476 AA [This is the length of the unprocessed precursor] Molecular weight: 52739 Da [This is the MW of the unprocessed precursor] CRC64: 4D11030800F2E163 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIYNMSTELF STLPYKVADI TLADFGRKEI DLAEKEMPGL MALREKYGES KPLKGARIMG 

        70         80         90        100        110        120 
SLHMTIQTAV LIETLVALGA EVRWCSCNIY STQDHAAAAI AASGVAVFAW KGENLADYWW 

       130        140        150        160        170        180 
CTLQALNFPG GKGPNVIVDD GGDATMMIHV GYDAENDAAV LDKEVHAEDE IELNAILKKV 

       190        200        210        220        230        240 
LAEDKTRWHR VAEEMRGVSE ETTTGVHRLY QMQEEGKLLF PAFNVNDSVT KSKFDNLYGC 

       250        260        270        280        290        300 
RESLADGIKR ATDVMIAGKV VVVCGYGDVG KGCSHSMRSY GARVLVTEVD PICALQAAME 

       310        320        330        340        350        360 
GFEVVTMEDA CTEGNIFVTT TGNIDIIRID HMEKMKDQAI VCNIGHFDNE IQVDALKHYS 

       370        380        390        400        410        420 
GIKCVNIKPQ VDRYYFPDGH SILLLADGRL VNLGCATGHP SFVMSNSFTN QTLAQIELFN 

       430        440        450        460        470 
KKYEVNVYRL PKHLDEEVAR LHLEKIGVKL TKLTPEQAAY IGVSVDGPYK AEHYRY 

Q8A407 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!