Reviewed, UniProtKB/Swiss-Prot Q8NSC4 (SAHH_CORGL)

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
Synonyms:	sahH
Ordered Locus Names:	Cgl0752, cg0860

Organism

Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	474 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; 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 compound 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 – 474	474	Adenosylhomocysteinase HAMAP MF_00563		PRO_0000116960
Regions
	Region	224 – 392	169	NAD binding By similarity
Sites
	Binding site	53	1	Substrate By similarity
	Binding site	135	1	Substrate By similarity
	Binding site	197	1	Substrate By similarity
	Binding site	227	1	Substrate By similarity
	Binding site	231	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8NSC4-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 74673F92624C4F9D	FASTA	474	51,996
	10 20 30 40 50 60 MDFKVADLSL AEAGRHQIRL AEYEMPGLMQ LRKEFADEQP LKGARIAGSI HMTVQTAVLI 70 80 90 100 110 120 ETLTALGAEV RWASCNIFST QDEAAAAIVV GSGTVEEPAG VPVFAWKGES LEEYWWCINQ 130 140 150 160 170 180 IFSWGDELPN MILDDGGDAT MAVIRGREYE QAGLVPPAEA NDSDEYIAFL GMLREVLAAE 190 200 210 220 230 240 PGKWGKIAEA VKGVTEETTT GVHRLYHFAE EGVLPFPAMN VNDAVTKSKF DNKYGTRHSL 250 260 270 280 290 300 IDGINRATDM LMGGKNVLVC GYGDVGKGCA EAFDGQGARV KVTEADPINA LQALMDGYSV 310 320 330 340 350 360 VTVDEAIEDA DIVITATGNK DIISFEQMLK MKDHALLGNI GHFDNEIDMH SLLHRDDVTR 370 380 390 400 410 420 TTIKPQVDEF TFSTGRSIIV LSEGRLLNLG NATGHPSFVM SNSFADQTIA QIELFQNEGQ 430 440 450 460 470 YENEVYRLPK VLDEKVARIH VEALGGQLTE LTKEQAEYIG VDVAGPFKPE HYRY

References

[1]

"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

[2]

"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000036 Genomic DNA. Translation: BAB98145.1. BX927150 Genomic DNA. Translation: CAF19456.1. Different initiation.
RefSeq	NP_599981.1. YP_225042.1.
3D structure databases
HSSP	HSSP built from PDB template 1B3R based on UniProtKB P10760.
ModBase	Search...
Genome annotation databases
GeneID	1018748. 3343536.
GenomeReviews	Gene locus Cgl0752 in contig BA000036_GR. Gene locus cg0860 in contig BX927147_GR.
KEGG	cgb:cg0860. cgl:NCgl0719.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8NSC4.
OMA	Q8NSC4. HMRAMKD.
Enzyme and pathway databases
BioCyc	CGLU196627-1:CG0860-MON.
BRENDA	3.3.1.1. 812.
Family and domain databases
HAMAP	MF_00563. [Tree]
InterPro	IPR000043. Ad_hcy_hydrolase. IPR015878. Ado_hCys_hydrolase_NAD-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.1480. Ad_hcy_hydrolase. 1 hit.
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_CORGL

Accession

Primary (citable) accession number: Q8NSC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 44 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)