Reviewed, UniProtKB/Swiss-Prot Q83A77 (SAHH_COXBU)

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:	CBU_2031

Organism

Coxiella burnetii [Complete proteome] [HAMAP]

Taxonomic identifier

777 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella

Protein attributes

Sequence length	438 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 – 438	438	Adenosylhomocysteinase HAMAP MF_00563		PRO_0000116961
Regions
	Region	191 – 356	166	NAD binding By similarity
Sites
	Binding site	64	1	Substrate By similarity
	Binding site	139	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	194	1	Substrate By similarity
	Binding site	198	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q83A77-1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: EF9BC88F62DA390F	FASTA	438	48,868
	10 20 30 40 50 60 MENDMETATM TQDYHIANIN LADWGRKEIE IAETEMPGLM ALRKKYKNAK PLKGARIAGC 70 80 90 100 110 120 IHMTIQTAVL IETLMLLGAE VRWSSCNIFS TQDHAAAALA QKGIPIFAWK GETEEEYWRC 130 140 150 160 170 180 IASTLEGPKG WTPNLLLDDG GDLTAHTLQK HPELCQNIRG VSEETTTGVH RLYRMLKEGS 190 200 210 220 230 240 LKFPAINVND SVTKSKFDNL YGCRESLIDS IKRATDVMIA GKRVVVCGYG DVGKGCAQSL 250 260 270 280 290 300 RAYGATVYIT EIDPICALQA AMEGYRVVTM DEMADSADIF VTATGNTDII THEHMLKMKD 310 320 330 340 350 360 QAIVCNIGHF DNEIDIASLQ DYQWMNIKPQ VDQVIFPDGK RLTVLAQGRL VNLGCATGHP 370 380 390 400 410 420 SFVMSNSFTN QVLAQIELWQ YPEKYPIGVY VLPKHLDEEV ARLHLERVGG KLTTLTEKQA 430 DYIGVDPEGP FKSEHYRY

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed: 12704232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nine Mile phase I / RSA 493.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016828 Genomic DNA. Translation: AAO91518.2.
RefSeq	NP_821004.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1209944.
GenomeReviews	Gene locus CBU_2031 in contig AE016828_GR.
KEGG	cbu:CBU_2031.
NMPDR	fig|227377.1.peg.1948.
TIGR	CBU_2031.
Phylogenomic databases
HOGENOM	HBG352029.
Enzyme and pathway databases
BioCyc	CBUR227377:CBU_2031-MONOMER.
BRENDA	3.3.1.1. 256353.
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]
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_COXBU

Accession

Primary (citable) accession number: Q83A77

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	December 16, 2008
Last modified:	February 9, 2010
This is version 49 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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