Reviewed, UniProtKB/Swiss-Prot O76757 (SAHH_ANOGA)

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:	Ahcy13
ORF Names:	AGAP000719

Organism

Anopheles gambiae (African malaria mosquito) [Complete proteome]

Taxonomic identifier

7165 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methinine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine By similarity.
Catalytic activity	S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.
Cofactor	Binds 1 NAD per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Sequence similarities	Belongs to the adenosylhomocysteinase family.

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 – 432	432	Adenosylhomocysteinase		PRO_0000116912
Regions
	Region	183 – 350	168	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	45	1	K → R in AAC29475. Ref.1
	Sequence conflict	92	1	A → V in AAC29475. Ref.1
	Sequence conflict	257	1	Y → K in AAC29475. Ref.1
	Sequence conflict	392	1	E → D in AAC29475. Ref.1
	Sequence conflict	414	1	A → P in AAC29475. Ref.1
	Sequence conflict	421	1	A → V in AAC29475. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O76757-1 [UniParc]. Last modified May 30, 2006. Version 2. Checksum: 6B384DCE94DDA1D3	FASTA	432	47,680
	10 20 30 40 50 60 MAKPAYKVAD ISLAEFGRKE IVLAENEMPG LMACRQKYGP LKILKGARIA GCLHMTIQTA 70 80 90 100 110 120 VLIETLIELG AEVQWSSCNI FSTQDHAAAA MAKAGVPVYA WKGETDEEYM WCIRQTLIFP 130 140 150 160 170 180 DGKPLNMILD DGGDLTNLVH AEHPELLKEI RGLSEETTTG VHNLYKMFRE GRLGMPAINV 190 200 210 220 230 240 NDSVTKSKFD NLYGCRESLL DGIKRATDVM IAGKVCVVAG YGDVGKGCAQ ALRGSGGRVL 250 260 270 280 290 300 ITEIDPINAL QAAMEGYEVT TMEEASKEAQ IFVTTTGCTD IIMGEHFLNM KDDSIVCNIG 310 320 330 340 350 360 HFDCEINVTW LQENAVEKVN IKPQVDRYRL ANGNHIILLA EGRLVNLGCA MGHSSFVMSN 370 380 390 400 410 420 SFTNQVLAQI ELWTNREQYA IGVHVLPKKL DEEVAALHLD KLGVKLTKLS ARQAEYLNLP 430 AEGPYKPEHY RY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The S-adenosyl-L-homocysteine hydrolase of Anopheles gambiae." Zhao Y., Lu W., Eggleston P. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: G3.
[2]	"The genome sequence of the malaria mosquito Anopheles gambiae." Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L. Science 298:129-149(2002) [PubMed: 12364791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PEST.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF080546 mRNA. Translation: AAC29475.1. AAAB01008847 Genomic DNA. Translation: EAA06909.2.
RefSeq	XP_311257.2.
3D structure databases
HSSP	HSSP built from PDB template 1LI4 based on UniProtKB P23526.
SMR	O76757. Positions 3-432.
ModBase	Search...
Protein-protein interaction databases
STRING	O76757.
Genome annotation databases
Ensembl	AGAP000719-RA; AGAP000719-PA; AGAP000719; Anopheles gambiae. [Genome view]
GeneID	1272312.
KEGG	aga:AgaP_AGAP000719.
VectorBase	AGAP000719. Anopheles gambiae.
Phylogenomic databases
HOGENOM	O76757.
OMA	LELWNER.
Enzyme and pathway databases
BRENDA	3.3.1.1. 165157.
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_ANOGA

Accession

Primary (citable) accession number: O76757
Secondary accession number(s): Q7QEC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	May 30, 2006
Last modified:	November 3, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)