Q13T36 (SAHH_BURXL) 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:	Bxeno_A4215
ORF Names:	Bxe_A0178

Organism

Burkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]

Taxonomic identifier

266265 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia

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
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_1000024721
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)
	Q13T36 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: E2D70FDD00B88386	FASTA	473	52,309
	10 20 30 40 50 60 MNAAVIDSKN SQDFIVADMS LADWGRKELN IAETEMPGLV QTREEYKVQQ PLKGARIAGS 70 80 90 100 110 120 LHMTIQTGVL IETLTALGAD VRWASCNIFS TQDHAAAAIA KAGTPVFAFK GESLDEYWEF 130 140 150 160 170 180 SHRIFEWPNG EFANMILDDG GDATLLLILG SKAEKDRSVI SKPTNEEEVA LYKSIERHLD 190 200 210 220 230 240 ADPTWYSTRL AHIKGVTEET TTGVHRLYQM EKEGRLPFPA INVNDSVTKS KFDNLYGCRE 250 260 270 280 290 300 SLVDGIKRAT DVMIAGKIAV VAGYGDVGKG CAQSLRGLGA TVWVTEIDPI CALQAAMEGY 310 320 330 340 350 360 RVVTMEYAAD KADIFVTATG NYHVIGHDHM KAMRHNAIVC NIGHFDSEID VASTRQYQWD 370 380 390 400 410 420 NIKPQVDHII FPDGKRVILL AEGRLVNLGC ATGHPSFVMS NSFTNQTLAQ IELFTQGNKY 430 440 450 460 470 ENKVYVLPKH LDEKVARLHL ARIGANLTVL SDEQAGYIGV DKNGPFKPNH YRY

References

[1]

"Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome shaped for versatility." Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., Parnell J.J. , Ramette A., Richardson P., Seeger M., Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M. Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006) [PubMed: 17030797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LB400.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000270 Genomic DNA. Translation: ABE32753.1.
RefSeq	YP_560805.1. NC_007951.1.
3D structure databases
ProteinModelPortal	Q13T36.
SMR	Q13T36. Positions 12-473.
ModBase	Search...
Protein-protein interaction databases
STRING	Q13T36.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4006249.
GenomeReviews	Gene locus Bxeno_A4215 in contig CP000270_GR.
KEGG	bxe:Bxe_A0178.
PATRIC	19334312. VBIBurXen52548_4433.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG352029.
OMA	SAQVWVT.
PhylomeDB	Q13T36.
ProtClustDB	PRK05476.
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_BURXL

Accession

Primary (citable) accession number: Q13T36

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	August 22, 2006
Last modified:	January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program