P35007 (SAHH_CATRO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenosylhomocysteinase
Short name=AdoHcyase
EC=3.3.1.1

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

Gene names

Name:

SAHH

Organism

Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)

Taxonomic identifier

4058 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Apocynaceae › Rauvolfioideae › Vinceae › Catharanthus

Protein attributes

Sequence length	485 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 By similarity.
Induction	By stress.
Sequence similarities	Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
Biological process	One-carbon metabolism Stress response
Ligand	NAD
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW
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 – 485	485	Adenosylhomocysteinase		PRO_0000116922
Regions
	Nucleotide binding	206 – 208	3	NAD By similarity
	Nucleotide binding	269 – 274	6	NAD By similarity
	Nucleotide binding	348 – 350	3	NAD By similarity
Sites
	Binding site	64	1	Substrate By similarity
	Binding site	139	1	Substrate By similarity
	Binding site	205	1	Substrate By similarity
	Binding site	235	1	Substrate By similarity
	Binding site	239	1	Substrate By similarity
	Binding site	240	1	NAD By similarity
	Binding site	292	1	NAD By similarity
	Binding site	327	1	NAD By similarity
	Binding site	397	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P35007 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 50CC0E99A9F66C51	FASTA	485	53,233
	10 20 30 40 50 60 MALLVEKTSS GREYKVKDMS QADFGRLEIE LAEVEMPGLM SCRAEFGPSQ PFKGAKITGS 70 80 90 100 110 120 LHMTIQTAVL IETLTALGAE VRWCSCNIFS TQEHAAAAIA RDSAAVFAWK GETLQEYWWC 130 140 150 160 170 180 TERALDWGPD GGPDLIVDDG GDATLLIHEG VKAEEEYKKN GALPDPSSTD NAEFQIVLTI 190 200 210 220 230 240 IRDGLKSDPT KYTRMKERLV GVSEETTTGV KRLYQMQANG TLLFPAINVN DSVTKSKFDN 250 260 270 280 290 300 LYGCRHSLPD GLMRATDVMI AGKVAVVAGY GDVGKGCAAA LKQAGARVIV TEIDPICALQ 310 320 330 340 350 360 ATMEGLQVLT LEDVVSEADI FVTTTGNKDI IMVDHMRKMK NNAIVCNIGH FDNEIDMLGL 370 380 390 400 410 420 ETYPGVKRIT IKPQTDRWVF PDTNSGIIVL AEGRLMNLGC ATGHPSFVMS CSFTNQVIAQ 430 440 450 460 470 480 LELWNERKTG KYEKKVYVLP KHLDEKVAAL HLGKLGAKLT KLTKDQADYI SVPIEGPYKP AHYRY

References

[1]	"cDNA for S-adenosyl-L-homocysteine hydrolase from Catharanthus roseus." Schroeder G., Waitz A., Hotze M., Schroeder J. Plant Physiol. 104:1099-1100(1994) [PubMed: 8165255] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z26881 mRNA. Translation: CAA81527.1.
PIR	S38379.
3D structure databases
ProteinModelPortal	P35007.
SMR	P35007. Positions 12-485.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR000043. Adenosylhomocysteinase. IPR015878. Ado_hCys_hydrolase_NAD-bd. IPR020082. S-Ado-L-homoCys_hydrolase_CS. [Graphical view]
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...

Entry information

Entry name

SAHH_CATRO

Accession

Primary (citable) accession number: P35007

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program