Q63PT2 (SAHH_BURPS) 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:	BPSL3290

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei)

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	473 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 MF_00563
Catalytic activity	S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine. HAMAP MF_00563
Cofactor	Binds 1 NAD per subunit By similarity. HAMAP MF_00563
Pathway	Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. HAMAP MF_00563
Subcellular location	Cytoplasm By similarity HAMAP MF_00563.
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: 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 – 473	473	Adenosylhomocysteinase HAMAP MF_00563		PRO_0000116954
Regions
	Nucleotide binding	200 – 202	3	NAD By similarity
	Nucleotide binding	263 – 268	6	NAD By similarity
	Nucleotide binding	342 – 344	3	NAD By similarity
Sites
	Binding site	64	1	Substrate By similarity
	Binding site	139	1	Substrate By similarity
	Binding site	199	1	Substrate By similarity
	Binding site	229	1	Substrate By similarity
	Binding site	233	1	Substrate By similarity
	Binding site	234	1	NAD By similarity
	Binding site	286	1	NAD By similarity
	Binding site	321	1	NAD By similarity
	Binding site	387	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63PT2 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 7A40ECDD0A47B596	FASTA	473	52,201
	10 20 30 40 50 60 MNAAVIDSHS AQDYVVADIA LAGWGRKELN IAETEMPGLV QIRDEYKAQQ PLKGARIAGS 70 80 90 100 110 120 LHMTIQTGVL IETLKALGAD VRWASCNIFS TQDHAAAAIV EAGTPVFAFK GESLDEYWEF 130 140 150 160 170 180 SHRIFEWPNG EFANMILDDG GDATLLLILG SKAEKDRSVI ARPTNEEEVA LFKSIERHLE 190 200 210 220 230 240 IDGSWYSKRL AHIKGVTEET TTGVHRLYQM EKDGRLPFPA FNVNDSVTKS KFDNLYGCRE 250 260 270 280 290 300 SLVDGIKRAT DVMIAGKIAV VAGYGDVGKG CAQSLRGLGA TVWVTEIDPI CALQAAMEGY 310 320 330 340 350 360 RVVTMEYAAD KADIFVTATG NYHVINHDHM KAMRHNAIVC NIGHFDSEID VASTRQYQWE 370 380 390 400 410 420 NIKPQVDHII FPDGKRVILL AEGRLVNLGC ATGHPSFVMS NSFTNQTLAQ IELFTRGGEY 430 440 450 460 470 ANKVYVLPKH LDEKVARLHL ARIGAQLSEL SDDQAAYIGV SKAGPFKPDH YRY

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571965 Genomic DNA. Translation: CAH37303.1.
RefSeq	YP_109886.1. NC_006350.1.
3D structure databases
ProteinModelPortal	Q63PT2.
SMR	Q63PT2. Positions 12-473.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3092196.
GenomeReviews	Gene locus BPSL3290 in contig BX571965_GR.
KEGG	bps:BPSL3290.
PATRIC	19267129. VBIBurPse99623_3743.
Phylogenomic databases
HOGENOM	HBG352029.
OMA	SAQVWVT.
PhylomeDB	Q63PT2.
ProtClustDB	PRK05476.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSL3290-MONOMER.
Family and domain databases
HAMAP	MF_00563. AdoHcyase. [Tree]
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_BURPS

Accession

Primary (citable) accession number: Q63PT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program