Reviewed, UniProtKB/Swiss-Prot Q8UJ99 (SAHH_AGRT5)

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:	Atu0029
ORF Names:	AGR_C_46

Organism

Agrobacterium tumefaciens (strain C58 / ATCC 33970) [Complete proteome] [HAMAP]

Taxonomic identifier

176299 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

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: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	adenosylhomocysteinase activity Inferred from electronic annotation. Source: HAMAP 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 – 466	466	Adenosylhomocysteinase HAMAP MF_00563		PRO_0000116939
Regions
	Region	219 – 384	166	NAD binding By similarity
Sites
	Binding site	57	1	Substrate By similarity
	Binding site	132	1	Substrate By similarity
	Binding site	192	1	Substrate By similarity
	Binding site	222	1	Substrate By similarity
	Binding site	226	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8UJ99-1 [UniParc]. Last modified June 6, 2002. Version 1. Checksum: 9A124B3304419F26	FASTA	466	51,160
	10 20 30 40 50 60 MSLEKDYIVA DINLAAFGRK ELDIAETEMP GLMSCRKEFG ESKPLKGARI TGSLHMTIQT 70 80 90 100 110 120 GVLIETLKEL GAEIRWASCN IFSTQDHAAA AIAAAGIPVF AVKGESLTEY WEYTDKIFQW 130 140 150 160 170 180 TDGGLSNMIL DDGGDATMYI LLGARAEAGE DVLSNPGSEE EEILFAQINK RLKASPGWFT 190 200 210 220 230 240 KQRDALKGVT EETTTGVHRL YDLAKKGLLP FPAINVNDSV TKSKFDNKYG CKESLVDGIR 250 260 270 280 290 300 RATDVMMAGK VAVVCGYGDV GKGSAASLQG AGARVKVTEI DPICALQAAM DGFEVVRLED 310 320 330 340 350 360 VVSSADIFIT TTGNKDVIRI EHMREMKDMA IVGNIGHFDN EIQVASLRNL KWTNIKPQVD 370 380 390 400 410 420 MIEFPKGNRI ILLSEGRLLN LGNATGHPSF VMSASFTNQV LGQIELFTKP GEYKNEVYVL 430 440 450 460 PKHLDEKVAR LHLEKLGVRL TELSDLQADY IGISKQGPFK AEHYRY

References

[1]

"The genome of the natural genetic engineer Agrobacterium tumefaciens C58." Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J. , Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., Nester E.W. Science 294:2317-2323(2001) [PubMed: 11743193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58." Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C. , Allinger M., Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S. Science 294:2323-2328(2001) [PubMed: 11743194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE007869 Genomic DNA. Translation: AAK85853.1.
PIR	AF2580. D97362.
RefSeq	NP_353068.1.
3D structure databases
SMR	Q8UJ99. Positions 5-466.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8UJ99.
Genome annotation databases
GeneID	1132067.
GenomeReviews	Gene locus Atu0029 in contig AE007869_GR.
KEGG	atc:AGR_C_46. atu:Atu0029.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0499.
HOGENOM	HBG352029.
OMA	VITHDHM.
PhylomeDB	Q8UJ99.
Enzyme and pathway databases
BioCyc	ATUM176299-1:ATU0029-MONOMER.
Family and domain databases
HAMAP	MF_00563_B. AdoHcyase_B. [Tree]
InterPro	IPR015878. Ado_hCys_hydrolase_NAD-bd. IPR016040. NAD(P)-bd_dom. IPR000043. S-Ado-L-homoCys_hydrolase. IPR020082. S-Ado-L-homoCys_hydrolase_CS. [Graphical view]
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.
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_AGRT5

Accession

Primary (citable) accession number: Q8UJ99

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	June 6, 2002
Last modified:	February 9, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)