Reviewed, UniProtKB/Swiss-Prot Q62G22 (SAHH_BURMA)

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:	BMA2842

Organism

Burkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP]

Taxonomic identifier

13373 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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 – 473	473	Adenosylhomocysteinase HAMAP MF_00563		PRO_0000116953
Regions
	Region	226 – 391	166	NAD binding 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

Sequences

	Sequence		Length	Mass (Da)
	Q62G22-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 7A40ECDD0A47B596	FASTA	473	52,201
	10 20 30 40 50 60 MNAAVIDSHS AQDYVVADIA LAGWGRKELN IAETEMPGLV QIRDEYKAQQ PLKGARIAGS 70 80 90 100 110 120 LHMTIQTGVL IETLKALGAD VRWASCNIFS TQDHAAAAIV EAGTPVFAFK GESLDEYWEF 130 140 150 160 170 180 SHRIFEWPNG EFANMILDDG GDATLLLILG SKAEKDRSVI ARPTNEEEVA LFKSIERHLE 190 200 210 220 230 240 IDGSWYSKRL AHIKGVTEET TTGVHRLYQM EKDGRLPFPA FNVNDSVTKS KFDNLYGCRE 250 260 270 280 290 300 SLVDGIKRAT DVMIAGKIAV VAGYGDVGKG CAQSLRGLGA TVWVTEIDPI CALQAAMEGY 310 320 330 340 350 360 RVVTMEYAAD KADIFVTATG NYHVINHDHM KAMRHNAIVC NIGHFDSEID VASTRQYQWE 370 380 390 400 410 420 NIKPQVDHII FPDGKRVILL AEGRLVNLGC ATGHPSFVMS NSFTNQTLAQ IELFTRGGEY 430 440 450 460 470 ANKVYVLPKH LDEKVARLHL ARIGAQLSEL SDDQAAYIGV SKAGPFKPDH YRY

References

[1]

"Structural flexibility in the Burkholderia mallei genome." Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E., Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M. , Kolonay J.F., Madupu R., Mohammoud Y., Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004) [PubMed: 15377793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 23344.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000010 Genomic DNA. Translation: AAU48323.1.
RefSeq	YP_104353.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3088686.
GenomeReviews	Gene locus BMA2842 in contig CP000010_GR.
KEGG	bma:BMA2842.
TIGR	BMA2842.
Phylogenomic databases
HOGENOM	Q62G22.
OMA	HMRAMKD.
Enzyme and pathway databases
BioCyc	BMAL243160:BMA_2842-MON.
BRENDA	3.3.1.1. 260531.
Family and domain databases
HAMAP	MF_00563. [Tree]
InterPro	IPR015878. Ado_hCys_hydrolase_NAD-bd. 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_BURMA

Accession

Primary (citable) accession number: Q62G22

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	October 25, 2004
Last modified:	November 3, 2009
This is version 37 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)