O13639 (SAHH_SCHPO) 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

ORF Names:

SPBC8D2.18c, pi047

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	433 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 By similarity.
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.
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	methionine metabolic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW selenocysteine metabolic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	adenosylhomocysteinase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 433	433	Adenosylhomocysteinase		PRO_0000116936
Regions
	Nucleotide binding	158 – 160	3	NAD By similarity
	Nucleotide binding	221 – 226	6	NAD By similarity
	Nucleotide binding	300 – 302	3	NAD By similarity
Sites
	Binding site	56	1	Substrate By similarity
	Binding site	132	1	Substrate By similarity
	Binding site	157	1	Substrate By similarity
	Binding site	187	1	Substrate By similarity
	Binding site	191	1	Substrate By similarity
	Binding site	192	1	NAD By similarity
	Binding site	244	1	NAD By similarity
	Binding site	347	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	O13639 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 8B4279CC2B518E13	FASTA	433	47,383
	10 20 30 40 50 60 MATQNYKVAD ISLAAFGRKE LEIAENEMPG LIAVREKYAK SQPLKGARIA GCLHMTIQTA 70 80 90 100 110 120 VLIETLVALG AEVTWSSCNI YSTQDHAAAA IAATGVPVFA WKGETEEEYL WCIEQQLKSF 130 140 150 160 170 180 PSGKPLNMIL DDGGDLTALV HERHPELLVD IRGISEETTT GVHNLYKMFK ENKLKVPAIN 190 200 210 220 230 240 VNDSVTKSKF DNLFGCKESL VDGIKRATDV MIAGKVAVVA GFGDVGKGCS TSLRSQGARV 250 260 270 280 290 300 IVTEVDPINA LQAAMDGFEV TTMEEAVKEG QIFVTTTGCR DIIRGEHFNE MKEDSIVCNI 310 320 330 340 350 360 GHFDVEIDVA WLKANAKDVV NIKPQVDRYE LKNGRHIILL ADGRLVNLGC ATGHPSFVMS 370 380 390 400 410 420 CSFTNQVLAQ IALWTDNTSY PLGVHMLPKK LDEEVARLHL GKLGVKLTTL TSVQSDYLGI 430 PVDGPYKADH YRY

References

[1]	"A 38 kb segment containing the cdc2 gene from the left arm of fission yeast chromosome II: sequence analysis and characterization of the genomic DNA and cDNAs encoded on the segment." Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K., Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y., Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M. Yeast 16:71-80(2000) [PubMed: 10620777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB004537 Genomic DNA. Translation: BAA21427.1. CU329671 Genomic DNA. Translation: CAA17833.1.
PIR	T40763.
RefSeq	NP_595580.1. NM_001021475.1.
3D structure databases
ProteinModelPortal	O13639.
SMR	O13639. Positions 6-433.
ModBase	Search...
Protein-protein interaction databases
STRING	O13639.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC8D2.18c.1; SPBC8D2.18c.1:pep; SPBC8D2.18c.
GeneID	2541218.
KEGG	spo:SPBC8D2.18c.
NMPDR	fig|4896.1.peg.1446.
Organism-specific databases
GeneDB_Spombe	SPBC8D2.18c.
Phylogenomic databases
eggNOG	fuNOG06806.
GeneTree	EFGT00050000003357.
HOGENOM	HBG352029.
OMA	SAQVWVT.
OrthoDB	EOG41G6CK.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003619-MONOMER.
Gene expression databases
ArrayExpress	O13639.
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...

Entry information

Entry name

SAHH_SCHPO

Accession

Primary (citable) accession number: O13639

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program