Skip Header

Contribute Send feedback
Read comments (?) or add your own

P60176 (SAHH_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:Rv3248c, MT3346
ORF Names:MTCY20B11.23c
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine By similarity. HAMAP-Rule MF_00563

Catalytic activity

S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine. HAMAP-Rule MF_00563

Cofactor

Binds 1 NAD per subunit. Ref.4

Pathway

Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. HAMAP-Rule MF_00563

Subunit structure

Homotetramer. Ref.4

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00563.

Sequence similarities

Belongs to the adenosylhomocysteinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 495494Adenosylhomocysteinase HAMAP-Rule MF_00563
PRO_0000116971

Regions

Nucleotide binding219 – 2213NAD By similarity
Nucleotide binding282 – 2876NAD By similarity
Nucleotide binding361 – 3633NAD By similarity

Sites

Binding site711Substrate By similarity
Binding site1561Substrate By similarity
Binding site2181Substrate By similarity
Binding site2481Substrate By similarity
Binding site2521Substrate By similarity
Binding site2531NAD By similarity
Binding site3051NAD By similarity
Binding site3401NAD By similarity
Binding site4091NAD By similarity

Amino acid modifications

Cross-link474Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) HAMAP-Rule MF_00563

Secondary structure

1 ............................................................................................ 495
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60176 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 386EF292620E7327

FASTA49554,324
        10         20         30         40         50         60 
MTGNLVTKNS LTPDVRNGID FKIADLSLAD FGRKELRIAE HEMPGLMSLR REYAEVQPLK 

        70         80         90        100        110        120 
GARISGSLHM TVQTAVLIET LTALGAEVRW ASCNIFSTQD HAAAAVVVGP HGTPDEPKGV 

       130        140        150        160        170        180 
PVFAWKGETL EEYWWAAEQM LTWPDPDKPA NMILDDGGDA TMLVLRGMQY EKAGVVPPAE 

       190        200        210        220        230        240 
EDDPAEWKVF LNLLRTRFET DKDKWTKIAE SVKGVTEETT TGVLRLYQFA AAGDLAFPAI 

       250        260        270        280        290        300 
NVNDSVTKSK FDNKYGTRHS LIDGINRGTD ALIGGKKVLI CGYGDVGKGC AEAMKGQGAR 

       310        320        330        340        350        360 
VSVTEIDPIN ALQAMMEGFD VVTVEEAIGD ADIVVTATGN KDIIMLEHIK AMKDHAILGN 

       370        380        390        400        410        420 
IGHFDNEIDM AGLERSGATR VNVKPQVDLW TFGDTGRSII VLSEGRLLNL GNATGHPSFV 

       430        440        450        460        470        480 
MSNSFANQTI AQIELWTKND EYDNEVYRLP KHLDEKVARI HVEALGGHLT KLTKEQAEYL 

       490 
GVDVEGPYKP DHYRY

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis."
Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E., Gygi S.P., Darwin K.H.
PLoS ONE 5:E8589-E8589(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PUPYLATION AT LYS-474, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: ATCC 25618 / H37Rv.
[4]"Crystal structures of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with substrate and inhibitors."
Reddy M.C., Kuppan G., Shetty N.D., Owen J.L., Ioerger T.R., Sacchettini J.C.
Protein Sci. 17:2134-2144(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD; ADENOSINE AND INHIBITORS, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000516 Genomic DNA. Translation: AAK47688.1.
AL123456 Genomic DNA. Translation: CCP46067.1.
PIRB70593.
RefSeqNP_217765.1. NC_000962.3.
NP_337874.1. NC_002755.2.
YP_006516724.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZIZX-ray2.20A/B/C/D1-495[»]
2ZJ0X-ray2.42A/B/C/D1-495[»]
2ZJ1X-ray2.01A/B/C/D1-495[»]
3CE6X-ray1.60A/B/C/D2-495[»]
3DHYX-ray2.00A/B/C/D1-495[»]
ProteinModelPortalP60176.
SMRP60176. Positions 10-495.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv3248c.

PTM databases

PhosSiteP12071732.

Proteomic databases

PaxDbP60176.
PRIDEP60176.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK47688; AAK47688; MT3346.
GeneID13318070.
888746.
922442.
KEGGmtc:MT3346.
mtu:Rv3248c.
PATRIC18129112. VBIMycTub22151_3652.

Organism-specific databases

TubercuListRv3248c.

Phylogenomic databases

eggNOGCOG0499.
HOGENOMHOG000227986.
KOK01251.
OMASAQVWVT.
ProtClustDBPRK05476.

Enzyme and pathway databases

UniPathwayUPA00314; UER00076.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00563. AdoHcyase.
InterProIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERPTHR23420. PTHR23420. 1 hit.
PfamPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
TIGRFAMsTIGR00936. ahcY. 1 hit.
PROSITEPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP60176.

Entry information

Entry nameSAHH_MYCTU
AccessionPrimary (citable) accession number: P60176
Secondary accession number(s): L0TBZ4, O08364, P81858
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: January 23, 2007
Last modified: May 29, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents