[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=8458573 [NCBI, ExPASy, EBI, Israel, Japan] Prasad S.S., Starr T., Rose A.M.; "Molecular characterization in the dpy-14 region identifies the adenosylhomocysteine hydrolase gene in Caenorhabditis elegans."; Genome 36:57-65(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Bristol N2; DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan] The C. elegans sequencing consortium; "Genome sequence of the nematode C. elegans: a platform for investigating biology."; Science 282:2012-2018(1998).

Comments

FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.
CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H₂O = L-homocysteine + adenosine.
COFACTOR: Binds 1 NAD per subunit.
PATHWAY: Amino-acid biosynthesis; homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1 .
SUBUNIT: Homotetramer.
INTERACTION:
Q09227:C08B11.9; NbExp=1; IntAct=EBI-314690, EBI-314686;
SIMILARITY: Belongs to the adenosylhomocysteinase family.

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

M64306; AAA28062.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S57284; AAB25906.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF043699; AAB97565.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T32918; T32918.

NP_491955.1; -.

3D structure databases

HSSP

P23526; 1LI4. [HSSP ENTRY / PDB]

SMR

P27604; 5-437.

ModBase

P27604.

Protein-protein interaction databases

DIP

DIP:25388N; -.

IntAct

P27604; -.

Organism-specific databases

WormBase

WBGene00019322; K02F2.2.

WormPep

K02F2.2; CE17154. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

P27604; -.

Ontologies

GO:0004013;	Molecular function: adenosylhomocysteinase activity (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0010171;	Biological process: body morphogenesis (inferred from mutant phenotype from WormBase).
GO:0009792;	Biological process: embryonic development ending in birth or egg hatching (inferred from mutant phenotype from WormBase).
GO:0040011;	Biological process: locomotion (inferred from mutant phenotype from WormBase).
GO:0040015;	Biological process: negative regulation of multicellular organism growth (inferred from mutant phenotype from WormBase).
GO:0002119;	Biological process: nematode larval development (inferred from mutant phenotype from WormBase).
GO:0006730;	Biological process: one-carbon compound metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

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.

Genome annotation databases

Ensembl

K02F2.2; Caenorhabditis elegans. [Contig view]

GeneID

172408; -.

KEGG

cel:K02F2.2; -.

Other

NextBio

875391; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Hydrolase; NAD; One-carbon metabolism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 437`	`437`	`Adenosylhomocysteinase.`	`PRO_0000116910`
`REGION`	`185 352`	`168`	`NAD binding (By similarity).`
`BINDING`	`58 58`		`Substrate (By similarity).`
`BINDING`	`133 133`		`Substrate (By similarity).`
`BINDING`	`158 158`		`Substrate (By similarity).`
`BINDING`	`188 188`		`Substrate (By similarity).`
`BINDING`	`192 192`		`Substrate (By similarity).`

Sequence information

Length: 437 AA [This is the length of the unprocessed precursor]

Molecular weight: 47536 Da [This is the MW of the unprocessed precursor]

CRC64: 53ADAB24507CFCD6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAQSKPAYKV ADIKLADFGR KEIILAENEM PGLMAMRSKY GPSQPLKGAR IAGCLHMTIQ 

        70         80         90        100        110        120 
TAVLIETLTA LGAEVQWSSC NIFSTQDHAA AAIAQTGVPV YAWKGETDEE YEWCIEQTIV 

       130        140        150        160        170        180 
FKDGQPLNMI LDDGGDLTNL VHAKYPQYLA GIRGLSEETT TGVHNLAKML AKGDLKVPAI 

       190        200        210        220        230        240 
NVNDSVTKSK FDNLYGIRES LPDGIKRATD VMLAGKVAVV AGYGDVGKGS AASLKAFGSR 

       250        260        270        280        290        300 
VIVTEIDPIN ALQAAMEGYE VTTLEEAAPK ANIIVTTTGC KDIVTGKHFE LLPNDAIVCN 

       310        320        330        340        350        360 
VGHFDCEIDV KWLNTNATKK DTIKPQVDRY TLKNGRHVIL LAEGRLVNLG CATGHPSFVM 

       370        380        390        400        410        420 
SNSFTNQVLA QVELWTKFGT PQEYKLGLYV LPKTLDEEVA YLHLAQLGVK LTKLSDEQAS 

       430 
YLGVPVAGPY KPDHYRY

P27604 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools