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Protein

Adenosylhomocysteinase

Gene

ahcY

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.UniRule annotation

Catalytic activityi

S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.UniRule annotation

Cofactori

NAD+UniRule annotation1 PublicationNote: Binds 1 NAD+ per subunit.UniRule annotation1 Publication

Pathwayi: L-homocysteine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-homocysteine from S-adenosyl-L-homocysteine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Adenosylhomocysteinase (ahcY), Adenosylhomocysteinase (ahcY)
This subpathway is part of the pathway L-homocysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homocysteine from S-adenosyl-L-homocysteine, the pathway L-homocysteine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei71 – 711SubstrateUniRule annotation
Binding sitei156 – 1561SubstrateUniRule annotation
Binding sitei218 – 2181SubstrateUniRule annotation
Binding sitei248 – 2481SubstrateUniRule annotation
Binding sitei252 – 2521SubstrateUniRule annotation
Binding sitei253 – 2531NADUniRule annotation
Binding sitei305 – 3051NADUniRule annotation
Binding sitei340 – 3401NADUniRule annotation
Binding sitei409 – 4091NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi219 – 2213NADUniRule annotation
Nucleotide bindingi282 – 2876NADUniRule annotation
Nucleotide bindingi361 – 3633NADUniRule annotation

GO - Molecular functioni

  • adenosylhomocysteinase activity Source: MTBBASE
  • NAD+ binding Source: MTBBASE

GO - Biological processi

  • adenosine metabolic process Source: MTBBASE
  • growth Source: MTBBASE
  • methionine catabolic process Source: MTBBASE
  • one-carbon metabolic process Source: UniProtKB-HAMAP
  • S-adenosylmethionine cycle Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00314; UER00076.

Names & Taxonomyi

Protein namesi
Recommended name:
AdenosylhomocysteinaseUniRule annotation (EC:3.3.1.1UniRule annotation)
Alternative name(s):
S-adenosyl-L-homocysteine hydrolaseUniRule annotation
Short name:
AdoHcyaseUniRule annotation
Gene namesi
Name:ahcYUniRule annotation
Synonyms:sahH
Ordered Locus Names:Rv3248c
ORF Names:MTCY20B11.23c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3248c.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytosol Source: MTBBASE
  • extracellular region Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495AdenosylhomocysteinasePRO_0000116971Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki474 – 474Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP9WGV3.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv3248c.

Structurei

Secondary structure

1
495
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 163Combined sources
Beta strandi19 – 224Combined sources
Helixi26 – 283Combined sources
Helixi29 – 4214Combined sources
Helixi44 – 5310Combined sources
Turni54 – 563Combined sources
Turni58 – 614Combined sources
Beta strandi63 – 686Combined sources
Helixi72 – 8312Combined sources
Beta strandi87 – 915Combined sources
Beta strandi93 – 964Combined sources
Helixi100 – 1089Combined sources
Turni109 – 1113Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi122 – 1243Combined sources
Helixi130 – 14112Combined sources
Beta strandi152 – 1587Combined sources
Helixi159 – 17315Combined sources
Helixi185 – 20016Combined sources
Helixi204 – 2118Combined sources
Beta strandi215 – 2173Combined sources
Helixi220 – 23112Combined sources
Beta strandi239 – 2413Combined sources
Helixi246 – 2494Combined sources
Helixi252 – 26918Combined sources
Beta strandi277 – 2815Combined sources
Helixi285 – 29612Combined sources
Beta strandi300 – 3045Combined sources
Helixi308 – 3169Combined sources
Helixi324 – 3274Combined sources
Helixi328 – 3303Combined sources
Beta strandi332 – 3365Combined sources
Beta strandi338 – 3414Combined sources
Helixi346 – 3516Combined sources
Beta strandi357 – 3604Combined sources
Beta strandi362 – 3643Combined sources
Helixi365 – 3673Combined sources
Helixi370 – 3756Combined sources
Beta strandi379 – 3846Combined sources
Beta strandi387 – 3915Combined sources
Turni393 – 3953Combined sources
Beta strandi398 – 4025Combined sources
Helixi403 – 4053Combined sources
Helixi408 – 4125Combined sources
Helixi418 – 43720Combined sources
Helixi439 – 4413Combined sources
Beta strandi444 – 4474Combined sources
Helixi451 – 46515Combined sources
Helixi474 – 4807Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP9WGV3.
SMRiP9WGV3. Positions 10-495.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the adenosylhomocysteinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C3E. Bacteria.
COG0499. LUCA.
KOiK01251.
OMAiKYGCRES.
PhylomeDBiP9WGV3.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00563. AdoHcyase.
InterProiIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERiPTHR23420. PTHR23420. 2 hits.
PfamiPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTiSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00936. ahcY. 1 hit.
PROSITEiPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P9WGV3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGNLVTKNS LTPDVRNGID FKIADLSLAD FGRKELRIAE HEMPGLMSLR
60 70 80 90 100
REYAEVQPLK GARISGSLHM TVQTAVLIET LTALGAEVRW ASCNIFSTQD
110 120 130 140 150
HAAAAVVVGP HGTPDEPKGV PVFAWKGETL EEYWWAAEQM LTWPDPDKPA
160 170 180 190 200
NMILDDGGDA TMLVLRGMQY EKAGVVPPAE EDDPAEWKVF LNLLRTRFET
210 220 230 240 250
DKDKWTKIAE SVKGVTEETT TGVLRLYQFA AAGDLAFPAI NVNDSVTKSK
260 270 280 290 300
FDNKYGTRHS LIDGINRGTD ALIGGKKVLI CGYGDVGKGC AEAMKGQGAR
310 320 330 340 350
VSVTEIDPIN ALQAMMEGFD VVTVEEAIGD ADIVVTATGN KDIIMLEHIK
360 370 380 390 400
AMKDHAILGN IGHFDNEIDM AGLERSGATR VNVKPQVDLW TFGDTGRSII
410 420 430 440 450
VLSEGRLLNL GNATGHPSFV MSNSFANQTI AQIELWTKND EYDNEVYRLP
460 470 480 490
KHLDEKVARI HVEALGGHLT KLTKEQAEYL GVDVEGPYKP DHYRY
Length:495
Mass (Da):54,324
Last modified:April 16, 2014 - v1
Checksum:i386EF292620E7327
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46067.1.
PIRiB70593.
RefSeqiNP_217765.1. NC_000962.3.
WP_003417039.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP46067; CCP46067; Rv3248c.
GeneIDi888746.
KEGGimtu:Rv3248c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46067.1.
PIRiB70593.
RefSeqiNP_217765.1. NC_000962.3.
WP_003417039.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP9WGV3.
SMRiP9WGV3. Positions 10-495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3248c.

Proteomic databases

PaxDbiP9WGV3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46067; CCP46067; Rv3248c.
GeneIDi888746.
KEGGimtu:Rv3248c.

Organism-specific databases

TubercuListiRv3248c.

Phylogenomic databases

eggNOGiENOG4105C3E. Bacteria.
COG0499. LUCA.
KOiK01251.
OMAiKYGCRES.
PhylomeDBiP9WGV3.

Enzyme and pathway databases

UniPathwayiUPA00314; UER00076.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00563. AdoHcyase.
InterProiIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERiPTHR23420. PTHR23420. 2 hits.
PfamiPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTiSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00936. ahcY. 1 hit.
PROSITEiPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "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.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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.

Entry informationi

Entry nameiSAHH_MYCTU
AccessioniPrimary (citable) accession number: P9WGV3
Secondary accession number(s): L0TBZ4
, O08364, P60176, P81858
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: February 17, 2016
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.