A9IGY5 (SAHH_BORPD) 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:	Bpet4763

Organism

Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]

Taxonomic identifier

340100 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	472 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
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 – 472	472	Adenosylhomocysteinase HAMAP MF_00563		PRO_1000129271
Regions
	Nucleotide binding	198 – 200	3	NAD By similarity
	Nucleotide binding	261 – 266	6	NAD By similarity
	Nucleotide binding	340 – 342	3	NAD By similarity
Sites
	Binding site	62	1	Substrate By similarity
	Binding site	137	1	Substrate By similarity
	Binding site	197	1	Substrate By similarity
	Binding site	227	1	Substrate By similarity
	Binding site	231	1	Substrate By similarity
	Binding site	232	1	NAD By similarity
	Binding site	284	1	NAD By similarity
	Binding site	319	1	NAD By similarity
	Binding site	385	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9IGY5 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: DF5C350F4277F2F3	FASTA	472	51,766
	10 20 30 40 50 60 MNAVSDQAVA DYHVADMSLA AWGRRELAIA ETEMPGLMAI REEFAASQPL KGARIAGSLH 70 80 90 100 110 120 MTIQTGVLIE TLVALGAEVR WASCNIFSTQ DHAAAAIAAT GTPVFAVKGE TLEEYWQYTH 130 140 150 160 170 180 RIFEWPEGRH ANMILDDGGD ATLLLHLGAR AEQDASVLAK PGSEEERVLF AAIKATLARD 190 200 210 220 230 240 PKWYSTRLAQ IRGVTEETTT GVHRLYQMAQ KGELAFAAIN VNDSVTKSKF DNLYGCRESL 250 260 270 280 290 300 VDGIKRATDV MVAGKIAVVA GYGDVGKGCA QALAALRAQV WVTEIDPICA LQAAMEGYKV 310 320 330 340 350 360 VTMEEAAPHA DIFVTATGNY HVITREHMQA MKDQAIVCNI GHFDNEIDVA ALDDCQWEEI 370 380 390 400 410 420 KPQVDHVVFP DGKRIILLAK GRLVNLGCAT GHPSFVMSSS FANQTIAQIE LYTRNEAYTR 430 440 450 460 470 GQVYVLPKHL DEKVARLHLK KLGAKLTSLR QDQADYINVP VEGPYKPDHY RY

References

[1]

"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae." Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R. BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-461 / DSM 12804 / CCUG 43448.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM902716 Genomic DNA. Translation: CAP45115.1.
RefSeq	YP_001633382.1. NC_010170.1.
3D structure databases
ProteinModelPortal	A9IGY5.
SMR	A9IGY5. Positions 11-472.
ModBase	Search...
Protein-protein interaction databases
STRING	A9IGY5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5820249.
GenomeReviews	Gene locus Bpet4763 in contig AM902716_GR.
KEGG	bpt:Bpet4763.
PATRIC	21171126. VBIBorPet31633_4789.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG352029.
OMA	SAQVWVT.
ProtClustDB	PRK05476.
Enzyme and pathway databases
BioCyc	BPET94624:BPET4763-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_BORPD

Accession

Primary (citable) accession number: A9IGY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program