Q72EH1 (SAHH_DESVH) 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:	DVU_0607

Organism

Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)

Taxonomic identifier

882 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio

Protein attributes

Sequence length	479 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 – 479	479	Adenosylhomocysteinase HAMAP MF_00563		PRO_0000116962
Regions
	Nucleotide binding	204 – 206	3	NAD By similarity
	Nucleotide binding	267 – 272	6	NAD By similarity
	Nucleotide binding	346 – 348	3	NAD By similarity
Sites
	Binding site	66	1	Substrate By similarity
	Binding site	142	1	Substrate By similarity
	Binding site	203	1	Substrate By similarity
	Binding site	233	1	Substrate By similarity
	Binding site	237	1	Substrate By similarity
	Binding site	238	1	NAD By similarity
	Binding site	290	1	NAD By similarity
	Binding site	325	1	NAD By similarity
	Binding site	394	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q72EH1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 27881713CC2C80B1	FASTA	479	52,897
	10 20 30 40 50 60 MTDAKRAQKL DLSLDHKVAD MSLADYGRKD LQLSEREMPG LMELIRKYGG TKPLKGLKVT 70 80 90 100 110 120 GSLHMTIQTA MLIRTLYELG ADIRWASCNI FSTQDHAAAA IAASGMAKVF AWKGETLEDY 130 140 150 160 170 180 WWCTEMALTW PDGSGPDLLV DDGGDATLFI HKGVEVENDP SLLKKAYDNK EFQIIMDRLA 190 200 210 220 230 240 LAYEQDPGRW QRVAAKVRGV SEETTTGVHR LYQLEQEGKL LFPAINVNDA VTKSKFDNLY 250 260 270 280 290 300 GCRESLADGI KRATDVMVAG KVVVVAGYGD VGKGCAQSMR GFGARVLVTE IDPICALQAA 310 320 330 340 350 360 MEGYEVTTME EAVRTGDIFV TATGNCNVIT GAHMEAMKDE AIVCNIGHFD NEIDMHYLEN 370 380 390 400 410 420 TEGCVCLNIK PQVDKWTLRS GRSIIVLAEG RLVNLGCATG HPSFVMSASF TNQTLAQIEL 430 440 450 460 470 ATNPDLERKV YTLPKKLDEE VARLHLDRLG VKLTRLSKDQ ADYIGVSPEG PFKPDHYRY

References

[1]

"The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough." Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Fouts D.E. , Haft D.H., Selengut J., Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M. Nat. Biotechnol. 22:554-559(2004) [PubMed: 15077118] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hildenborough / ATCC 29579 / NCIMB 8303.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017285 Genomic DNA. Translation: AAS95088.1.
RefSeq	YP_009829.1. NC_002937.3.
3D structure databases
ProteinModelPortal	Q72EH1.
SMR	Q72EH1. Positions 15-479.
ModBase	Search...
Protein-protein interaction databases
STRING	Q72EH1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2793368.
GenomeReviews	Gene locus DVU_0607 in contig AE017285_GR.
KEGG	dvu:DVU0607.
PATRIC	32061156. VBIDesVul119526_0569.
TIGR	DVU_0607.
Phylogenomic databases
eggNOG	COG0499.
HOGENOM	HBG352029.
OMA	SAQVWVT.
PhylomeDB	Q72EH1.
ProtClustDB	PRK05476.
Enzyme and pathway databases
BioCyc	DVUL882:DVU_0607-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_DESVH

Accession

Primary (citable) accession number: Q72EH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program