Reviewed, UniProtKB/Swiss-Prot P10819 (SAHH_DICDI)

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:	sahA
ORF Names:	DDB_G0267418

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Sequence caution	The sequence CAA31040.1 differs from that shown. Reason: Frameshift at position 270.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	NAD
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	adenosylhomocysteinase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 431	431	Adenosylhomocysteinase		PRO_0000116911
Regions
	Region	183 – 349	167	NAD binding By similarity
Sites
	Binding site	56	1	Substrate By similarity
	Binding site	131	1	Substrate By similarity
	Binding site	156	1	Substrate By similarity
	Binding site	186	1	Substrate By similarity
	Binding site	190	1	Substrate By similarity
Experimental info
	Sequence conflict	25	1	E → A in AAA33165. Ref.1
	Sequence conflict	123	1	Missing in AAA33165. Ref.1
	Sequence conflict	137	1	N → T in AAA33165. Ref.1
	Sequence conflict	159	1	T → H in AAA33165. Ref.1
	Sequence conflict	313	1	A → G in CAA31040. Ref.3
	Sequence conflict	325	1	D → S in CAA31040. Ref.3
	Sequence conflict	361 – 365	5	FCNQT → SVTK in CAA31040. Ref.3
	Sequence conflict	384	1	F → L in AAA33165. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P10819-1 [UniParc]. Last modified December 4, 2007. Version 2. Checksum: C621FC6BE5BCBA2A	FASTA	431	47,280
	10 20 30 40 50 60 MTKLHYKVKD ISLAAWGRKE IEIAENEMPG LMTLRKKYGP AQILKGARIA GCLHMTIQTA 70 80 90 100 110 120 VLIETLTALG AQVQWSSCNI FSTQDQAAAA IAATGVPVYA WKGETEEEYN WCVEQTIVFQ 130 140 150 160 170 180 DGQPLNMILD DGGDLTNLVH EKYPQFLAGI KGISEETTTG VHNLYKMFKE GKLKVPAINV 190 200 210 220 230 240 NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ SLSKMGARVL 250 260 270 280 290 300 VTEIDPINAL QACMDGYQIV TMETAAPLSN IFVTTTGCRD IVRGEHFAVM KEDAIVCNIG 310 320 330 340 350 360 HFDCEIDVAW LNANAKKDTV KPQVDRYTLA NGVHIILLAE GRLVNLGCGT GHPSFVMSNS 370 380 390 400 410 420 FCNQTLAQIA LWTKTEEYPL GVHFLPKILD EEVARLHLDQ LGAKLTTLTE KQSEYLSVPV 430 AGPYKVDHYR Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Amino acid sequence of S-adenosyl-L-homocysteine hydrolase from Dictyostelium discoideum as deduced from the cDNA sequence." Kasir J., Aksamit R.R., Backlund P.S. Jr., Cantoni G.L. Biochem. Biophys. Res. Commun. 153:359-364(1988) [PubMed: 3288206] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"Cloning of a cDNA for the S-adenosyl-L-homocysteine hydrolase from Dictyostelium discoideum." Guitton M.C., Part D., Veron M. Biochimie 70:835-840(1988) [PubMed: 3139100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 256-431.
[4]	"Identification and isolation of Dictyostelium microtubule-associated protein interactors by tandem affinity purification." Koch K.V., Reinders Y., Ho T.-H., Sickmann A., Graef R. Eur. J. Cell Biol. 85:1079-1090(2006) [PubMed: 16782229] [Abstract] Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]	"Proteomics fingerprinting of phagosome maturation and evidence for the role of a Galpha during uptake." Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M., Soldati T. Mol. Cell. Proteomics 5:2228-2243(2006) [PubMed: 16926386] [Abstract] Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M19937 mRNA. Translation: AAA33165.1. AAFI02000003 Genomic DNA. Translation: EAL73161.1. X12523 mRNA. Translation: CAA31040.1. Frameshift.
PIR	A27655.
RefSeq	XP_647635.1.
3D structure databases
HSSP	HSSP built from PDB template 1LI4 based on UniProtKB P23526.
SMR	P10819. Positions 3-430.
ModBase	Search...
Protein-protein interaction databases
STRING	P10819.
Genome annotation databases
GeneID	3398816.
GenomeReviews	Gene locus sahA in contig CM000150_GR.
KEGG	ddi:DDB_0191108.
Organism-specific databases
dictyBase	DDB_G0267418. sahA.
Phylogenomic databases
OMA	HMRAMKD.
Enzyme and pathway databases
BRENDA	3.3.1.1. 424.
Family and domain databases
InterPro	IPR015878. Ado_hCys_hydrolase_NAD-bd. IPR000043. S-Ado-L-homoCys_hydrolase. 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.
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_DICDI

Accession

Primary (citable) accession number: P10819
Secondary accession number(s): Q55F98

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	December 4, 2007
Last modified:	November 3, 2009
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)