P61617 (SAHH_GEOSL) 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:	GSU1875

Organism

Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)

Taxonomic identifier

243231 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfuromonadales › Geobacteraceae › Geobacter

Protein attributes

Sequence length	475 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 – 475	475	Adenosylhomocysteinase HAMAP MF_00563		PRO_0000116963
Regions
	Nucleotide binding	202 – 204	3	NAD By similarity
	Nucleotide binding	265 – 270	6	NAD By similarity
	Nucleotide binding	344 – 346	3	NAD By similarity
Sites
	Binding site	66	1	Substrate By similarity
	Binding site	141	1	Substrate By similarity
	Binding site	201	1	Substrate By similarity
	Binding site	231	1	Substrate By similarity
	Binding site	235	1	Substrate By similarity
	Binding site	236	1	NAD By similarity
	Binding site	288	1	NAD By similarity
	Binding site	323	1	NAD By similarity
	Binding site	389	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P61617 [UniParc]. Last modified May 24, 2004. Version 1. Checksum: 525470CE91067817	FASTA	475	52,284
	10 20 30 40 50 60 MTQPVARDTA GTFSDYCISD ISLAAWGRKE MIIAETEMPG LMAIREEYAA TRPLQGARIA 70 80 90 100 110 120 GSLHMTIQTA MLIETLVALG AEVRWASCNI FSTQDHAAAA IAAAGIPVFA YKGESLEEYW 130 140 150 160 170 180 EFTHRIFEWH DGGTPNMILD DGGDATLLLH LGSDAEKDPS VIANPTCEEE QYLFASIKKR 190 200 210 220 230 240 LAEKPGWYSK TAAAIKGVTE ETTTGVHRLY QMHEKGKLKF PAINVNDSVT KSKFDNIYGC 250 260 270 280 290 300 RESLVDGIKR ATDVMIAGKV AVICGYGEVG KGCAQAMRGL QAQVWVTEID PICALQAAME 310 320 330 340 350 360 GYRVVTMEYA ADKADIFVTT TGNINVITHD HMKAMRHNAI VCNIGHFDNE IEVAALKQYQ 370 380 390 400 410 420 WENIKPQVDH IIFPDSKRII LLAEGRLVNL GCATGHPSYV MSSSFANQTL AQIELFCNPG 430 440 450 460 470 KYPVGVYMLP KELDEKVARL QLKTLGAMLT ELTDEQAAYI GVPKNGPYKS AHYRY

References

[1]

"Genome of Geobacter sulfurreducens: metal reduction in subsurface environments." Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C., Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J., Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.L., Kolonay J.F. , Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R., Fraser C.M. Science 302:1967-1969(2003) [PubMed: 14671304] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51573 / DSM 12127 / PCA.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017180 Genomic DNA. Translation: AAR35251.1.
RefSeq	NP_952924.1. NC_002939.4.
3D structure databases
ProteinModelPortal	P61617.
SMR	P61617. Positions 15-475.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2685778.
GenomeReviews	Gene locus GSU1875 in contig AE017180_GR.
KEGG	gsu:GSU1875.
NMPDR	fig|243231.1.peg.1862.
PATRIC	22026615. VBIGeoSul17553_1913.
TIGR	GSU1875.
Phylogenomic databases
HOGENOM	HBG352029.
OMA	SAQVWVT.
PhylomeDB	P61617.
ProtClustDB	PRK05476.
Enzyme and pathway databases
BioCyc	GSUL243231:GSU_1875-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_GEOSL

Accession

Primary (citable) accession number: P61617

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	May 24, 2004
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program