A5E357 (A5E357_LODEL) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Adenosylhomocysteinase RuleBase RU000548
EC=3.3.1.1 RuleBase RU000548

Gene names

ORF Names:

LELG_04044 EMBL EDK45865.1

Organism

Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) [Complete proteome] EMBL EDK45865.1

Taxonomic identifier

379508 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Lodderomyces › Lodderomyces elongisporus

Protein attributes

Sequence length	446 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine. RuleBase RU000548
Cofactor	Binds 1 NAD per subunit By similarity. RuleBase RU000548
Pathway	Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. RuleBase RU000548
Sequence similarities	Belongs to the adenosylhomocysteinase family. RuleBase RU004166

Ontologies

Keywords
Biological process	One-carbon metabolism RuleBase RU000548
Ligand	NAD RuleBase RU000548
Molecular function	Hydrolase RuleBase RU000548
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 nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Binding site	55	1	Substrate By similarity PIRSR PIRSR001109-1
	Binding site	131	1	Substrate By similarity PIRSR PIRSR001109-1
	Binding site	156	1	Substrate By similarity PIRSR PIRSR001109-1
	Binding site	186	1	Substrate By similarity PIRSR PIRSR001109-1
	Binding site	190	1	Substrate By similarity PIRSR PIRSR001109-1

Sequences

	Sequence		Length	Mass (Da)
	A5E357 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 792EDCADF4D9DB0D	FASTA	446	48,823
	10 20 30 40 50 60 MASNYKVADI SLAAFGRKDI ELSENEMPGL MYIRKKYGPS QPLKGARIAG CLHMTIQTAV 70 80 90 100 110 120 LIETLVALGA EVTWTSCNIF STQDHAAAAI AAAGVPVFAW KGETEEEYQW CIEQQLFAFK 130 140 150 160 170 180 DGKKLNLILD DGGDLTSLVH EKYPEMLEDC YGLSEETTTG VHHLYKALRD GKLKVPAINV 190 200 210 220 230 240 NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG FGDVGKGCAM ALQGMGARVI 250 260 270 280 290 300 VTEIDPINAL QAAVSGYQVA PLDEVASIGQ IFVTTTGCRD IIVGKHFEKM PEDAIVCNIG 310 320 330 340 350 360 HFDIEIDVAW LKANAESVVN IKPQVDRYLM KNGRHIILLA DGRLVNLGCA TGHSSFVMSC 370 380 390 400 410 420 SFSNQVLAQI ALFNDKNKEF KEKFPEFAKT GPFDVNVHLL PKILDETVAK CHLDHLNARL 430 440 TTLTDVQAEY LGIPKEGPFK ADIYRY

References

[1]

"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH981528 Genomic DNA. Translation: EDK45865.1.
RefSeq	XP_001525012.1. XM_001524962.1.
3D structure databases
ProteinModelPortal	A5E357.
SMR	A5E357. Positions 5-446.
ModBase	Search...
Protein-protein interaction databases
STRING	36914.A5E357.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5231904.
KEGG	lel:LELG_04044.
Phylogenomic databases
KO	K01251.
OMA	TIGMALH.
OrthoDB	EOG41G6CK.
Enzyme and pathway databases
UniPathway	UPA00314; UER00076.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_00563. AdoHcyase.
InterPro	IPR000043. Adenosylhomocysteinase. IPR015878. Ado_hCys_hydrolase_NAD-bd. IPR016040. NAD(P)-bd_dom. IPR020082. S-Ado-L-homoCys_hydrolase_CS. [Graphical view]
PANTHER	PTHR23420. PTHR23420. 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

A5E357_LODEL

Accession

Primary (citable) accession number: A5E357

Entry history

Integrated into UniProtKB/TrEMBL:	June 12, 2007
Last sequence update:	June 12, 2007
Last modified:	April 3, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)