P27604 (SAHH_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenosylhomocysteinase
Short name=AdoHcyase
EC=3.3.1.1

Alternative name(s):
Protein dumpy-14
S-adenosyl-L-homocysteine hydrolase

Gene names

Name:	ahcy-1
Synonyms:	ahh, dpy-14
ORF Names:	K02F2.2

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	NAD
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	body morphogenesis Inferred from mutant phenotype. Source: WormBase embryo development ending in birth or egg hatching Inferred from mutant phenotype. Source: WormBase growth Inferred from mutant phenotype. Source: WormBase locomotion Inferred from mutant phenotype. Source: WormBase negative regulation of multicellular organism growth Inferred from mutant phenotype. Source: WormBase nematode larval development Inferred from mutant phenotype. Source: WormBase one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW receptor-mediated endocytosis Inferred from mutant phenotype. Source: WormBase secretion by cell Inferred from mutant phenotype. Source: WormBase
Molecular function	adenosylhomocysteinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 437	437	Adenosylhomocysteinase		PRO_0000116910
Regions
	Nucleotide binding	159 – 161	3	NAD By similarity
	Nucleotide binding	224 – 229	6	NAD By similarity
	Nucleotide binding	301 – 303	3	NAD By similarity
Sites
	Binding site	58	1	Substrate By similarity
	Binding site	133	1	Substrate By similarity
	Binding site	158	1	Substrate By similarity
	Binding site	188	1	Substrate By similarity
	Binding site	192	1	Substrate By similarity
	Binding site	193	1	NAD By similarity
	Binding site	245	1	NAD By similarity
	Binding site	348	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27604 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 53ADAB24507CFCD6	FASTA	437	47,536
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization in the dpy-14 region identifies the adenosylhomocysteine hydrolase gene in Caenorhabditis elegans." Prasad S.S., Starr T., Rose A.M. Genome 36:57-65(1993) [PubMed: 8458573] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M64306 Genomic DNA. Translation: AAA28062.1. S57284 Genomic DNA. Translation: AAB25906.1. FO081029 Genomic DNA. Translation: CCD68626.1.
PIR	T32918.
RefSeq	NP_491955.1. NM_059554.5.
UniGene	Cel.7612.
3D structure databases
ProteinModelPortal	P27604.
SMR	P27604. Positions 5-437.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-25388N.
IntAct	P27604. 1 interaction.
MINT	MINT-1076618.
STRING	P27604.
2D gel databases
World-2DPAGE	0011:P27604. 0020:P27604.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	K02F2.2.1; K02F2.2.1; K02F2.2. K02F2.2.2; K02F2.2.2; K02F2.2.
GeneID	172408.
KEGG	cel:K02F2.2.
UCSC	K02F2.2.1. c. elegans.
Organism-specific databases
CTD	172408.
WormBase	K02F2.2; CE17154; WBGene00019322; ahcy-1.
Phylogenomic databases
eggNOG	meNOG04936.
GeneTree	EMGT00050000015433.
HOGENOM	HBG352029.
InParanoid	P27604.
OMA	ELFTKTE.
PhylomeDB	P27604.
Gene expression databases
ArrayExpress	P27604.
Family and domain databases
InterPro	IPR000043. Adenosylhomocysteinase. IPR015878. Ado_hCys_hydrolase_NAD-bd. IPR020082. S-Ado-L-homoCys_hydrolase_CS. [Graphical view]
KO	K01251.
PANTHER	PTHR23420. Ad_hcy_hydrolase. 1 hit.
Pfam	PF05221. AdoHcyase. 1 hit. PF00670. AdoHcyase_NAD. 1 hit. [Graphical view]
PIRSF	PIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMART	SM00996. AdoHcyase. 1 hit. SM00997. AdoHcyase_NAD. 1 hit. [Graphical view]
TIGRFAMs	TIGR00936. AhcY. 1 hit.
PROSITE	PS00738. ADOHCYASE_1. 1 hit. PS00739. ADOHCYASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	875391.

Entry information

Entry name

SAHH_CAEEL

Accession

Primary (citable) accession number: P27604

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	January 25, 2012
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project