P83783 (SAHH_CANAL) 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:	SAH1
ORF Names:	CaO19.3911, CaO19.11392

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	450 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 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.
Subcellular location	Cytoplasm Ref.2.
Miscellaneous	Has antigenic properties. Elicits a specific immune response in systemic candidiasis human patients undergoing malignant hematological disorders.
Sequence similarities	Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 450	450	Adenosylhomocysteinase		PRO_0000116934
Regions
	Nucleotide binding	161 – 163	3	NAD By similarity
	Nucleotide binding	224 – 229	6	NAD By similarity
	Nucleotide binding	303 – 305	3	NAD By similarity
Sites
	Binding site	59	1	Substrate By similarity
	Binding site	135	1	Substrate By similarity
	Binding site	160	1	Substrate By similarity
	Binding site	190	1	Substrate By similarity
	Binding site	194	1	Substrate By similarity
	Binding site	195	1	NAD By similarity
	Binding site	247	1	NAD By similarity
	Binding site	350	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P83783 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 85A6D18CE85517E3	FASTA	450	49,072
	10 20 30 40 50 60 MSSAPATNYK VADISLAAFG RKDIELSENE MPGLMYIRKK YGPSQPLKGA RIAGCLHMTI 70 80 90 100 110 120 QTAVLIETLV ALGAEVTWSS CNIFSTQDHA AAAIAAAGVP VFAWKGETEE EYQWCIEQQL 130 140 150 160 170 180 FAFKDGKKLN LILDDGGDLT SLVHEKYPEM LEDCYGLSEE TTTGVHHLYK SLRDGKLKVP 190 200 210 220 230 240 AINVNDSVTK SKFDNLYGCR ESLVDGIKRA TDVMIAGKVA IVAGFGDVGK GCAMALHGMG 250 260 270 280 290 300 ARVIVTEIDP INALQAAVSG YQVAPMDEVA SIGQIFVTTT GCRDIITGKH FEQMPEDAIV 310 320 330 340 350 360 CNIGHFDIEI DVAWLKANAE SVVNIKPQVD RYLMKNGRHV ILLADGRLVN LGCATGHSSF 370 380 390 400 410 420 VMSCSFSNQV LAQIALFNAD NKEFREKFPE FAKTGPFDVG VHLLPKVLDE TVARCHLDHL 430 440 450 GAKLTTLTET QAEYLGIPEE GPYKADIYRY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314 / ATCC MYA-2876.
[2]	"Proteomics-based identification of novel Candida albicans antigens for diagnosis of systemic candidiasis in patients with underlying hematological malignancies." Pitarch A., Abian J., Carrascal M., Sanchez M., Nombela C., Gil C. Proteomics 4:3084-3106(2004) [PubMed: 15378761] [Abstract] Cited for: PROTEIN SEQUENCE OF 179-190 AND 193-200, SUBCELLULAR LOCATION, ANTIGENICITY. Strain: SC5314 / ATCC MYA-2876. Tissue: Protoplast.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACQ01000012 Genomic DNA. Translation: EAL03041.1. AACQ01000011 Genomic DNA. Translation: EAL03204.1.
RefSeq	XP_721821.1. XM_716728.1. XP_721980.1. XM_716887.1.
3D structure databases
ProteinModelPortal	P83783.
SMR	P83783. Positions 9-450.
ModBase	Search...
Protein-protein interaction databases
STRING	P83783.
2D gel databases
COMPLUYEAST-2DPAGE	P83783.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3636277. 3636452.
KEGG	cal:CaO19.11392. cal:CaO19.3911.
Organism-specific databases
CGD	CAL0002855. SAH1.
Phylogenomic databases
OMA	GCAEAMA.
PhylomeDB	P83783.
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_CANAL

Accession

Primary (citable) accession number: P83783
Secondary accession number(s): Q5AKA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	May 5, 2009
Last modified:	January 25, 2012
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program