Q58783 (SAHH_METJA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenosylhomocysteinase
EC=3.3.1.1

Alternative name(s):
S-adenosyl-L-homocysteine hydrolase
Short name=AdoHcyase

Gene names

Name:	ahcY
Ordered Locus Names:	MJ1388

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus › Methanocaldococcus jannaschii

Protein attributes

Sequence length	415 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine By similarity. HAMAP-Rule MF_00563
Catalytic activity	S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine. HAMAP-Rule MF_00563
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. HAMAP-Rule MF_00563
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	one-carbon metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	adenosylhomocysteinase activity Inferred from electronic annotation. Source: HAMAP nucleotide 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 – 415	415	Adenosylhomocysteinase HAMAP-Rule MF_00563		PRO_0000117004
Regions
	Nucleotide binding	149 – 151	3	NAD By similarity
	Nucleotide binding	212 – 217	6	NAD By similarity
	Nucleotide binding	291 – 293	3	NAD By similarity
Sites
	Binding site	123	1	Substrate By similarity
	Binding site	148	1	Substrate By similarity
	Binding site	178	1	Substrate By similarity
	Binding site	182	1	Substrate By similarity
	Binding site	183	1	NAD By similarity
	Binding site	235	1	NAD By similarity
	Binding site	337	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q58783 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 16B1456E74D180F5	FASTA	415	46,607
	10 20 30 40 50 60 MYEVRDINLW KEGERKIQWA KQHMPVLNLI RERFKEEKPF KGITIGMALH LEAKTAVLAE 70 80 90 100 110 120 TLMEGGAEIA ITGCNPLSTQ DDVAAACAKK GMHVYAWRGE TVEEYYENLN KVLDHKPDIV 130 140 150 160 170 180 IDDGCDLIFL LHTKRTELLD NIMGGCEETT TGIIRLKAME KEGALKFPVM DVNDAYTKHL 190 200 210 220 230 240 FDNRYGTGQS ALDGILRATN LLIAGKTVVV AGYGWCGRGV AMRAKGLGAE VVVTEVNPIR 250 260 270 280 290 300 ALEARMDGFR VMKMEKAAEI GDIFITTTGC KDVIRKEHIL KMRNGAILAN AGHFDNEINK 310 320 330 340 350 360 KHLEELAKSI KEVRNCVTEY DLGNKKIYLL GEGRLVNLAC ADGHPCEVMD MSFANQALAA 370 380 390 400 410 EYILKNHEKL EPRVYNIPYE QDLMIASLKL KAMGIEIDEL TKEQKKYLED WREGT

References

[1]

"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L77117 Genomic DNA. Translation: AAB99397.1.
PIR	C64473.
RefSeq	NP_248391.1. NC_000909.1.
3D structure databases
ProteinModelPortal	Q58783.
ModBase	Search...
Protein-protein interaction databases
STRING	243232.MJ1388.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB99397; AAB99397; MJ_1388.
GeneID	1452291.
KEGG	mja:MJ_1388.
Phylogenomic databases
eggNOG	COG0499.
KO	K01251.
OMA	TIGMALH.
ProtClustDB	PRK05476.
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

SAHH_METJA

Accession

Primary (citable) accession number: Q58783

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program