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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)DescriptionActionsGraphical viewLength
Binding sitei71SubstrateUniRule annotation1
Binding sitei156SubstrateUniRule annotation1
Binding sitei218SubstrateUniRule annotation1
Binding sitei248SubstrateUniRule annotation1
Binding sitei252SubstrateUniRule annotation1
Binding sitei253NADUniRule annotation1
Binding sitei305NADUniRule annotation1
Binding sitei340NADUniRule annotation1
Binding sitei409NADUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi219 – 221NADUniRule annotation3
Nucleotide bindingi282 – 287NADUniRule annotation6
Nucleotide bindingi361 – 363NADUniRule annotation3

GO - Molecular functioni

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

GO - Biological processi

  • adenosine metabolic process Source: MTBBASE
  • adhesion of symbiont to host cell Source: AgBase
  • entry of bacterium into host cell Source: AgBase
  • growth Source: MTBBASE
  • methionine catabolic process Source: MTBBASE
  • one-carbon metabolic process Source: UniProtKB-HAMAP
  • S-adenosylhomocysteine catabolic process Source: InterPro
  • 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

BioCyciMTBH37RV:G185E-7522-MONOMER.
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001169711 – 495AdenosylhomocysteinaseAdd BLAST495

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki474Isoglutamyl 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

Binary interactionsi

WithEntry#Exp.IntActNotes
CXCL8P101453EBI-11740468,EBI-3917999From a different organism.

Protein-protein interaction databases

IntActiP9WGV3. 1 interactor.
STRINGi83332.Rv3248c.

Structurei

Secondary structure

1495
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 16Combined sources3
Beta strandi19 – 22Combined sources4
Helixi26 – 28Combined sources3
Helixi29 – 42Combined sources14
Helixi44 – 53Combined sources10
Turni54 – 56Combined sources3
Turni58 – 61Combined sources4
Beta strandi63 – 68Combined sources6
Helixi72 – 83Combined sources12
Beta strandi87 – 91Combined sources5
Beta strandi93 – 96Combined sources4
Helixi100 – 108Combined sources9
Turni109 – 111Combined sources3
Beta strandi114 – 116Combined sources3
Beta strandi122 – 124Combined sources3
Helixi130 – 141Combined sources12
Beta strandi152 – 158Combined sources7
Helixi159 – 173Combined sources15
Helixi185 – 200Combined sources16
Helixi204 – 211Combined sources8
Beta strandi215 – 217Combined sources3
Helixi220 – 231Combined sources12
Beta strandi239 – 241Combined sources3
Helixi246 – 249Combined sources4
Helixi252 – 269Combined sources18
Beta strandi277 – 281Combined sources5
Helixi285 – 296Combined sources12
Beta strandi300 – 304Combined sources5
Helixi308 – 316Combined sources9
Helixi324 – 327Combined sources4
Helixi328 – 330Combined sources3
Beta strandi332 – 336Combined sources5
Beta strandi338 – 341Combined sources4
Helixi346 – 351Combined sources6
Beta strandi357 – 360Combined sources4
Beta strandi362 – 364Combined sources3
Helixi365 – 367Combined sources3
Helixi370 – 375Combined sources6
Beta strandi379 – 384Combined sources6
Beta strandi387 – 391Combined sources5
Turni393 – 395Combined sources3
Beta strandi398 – 402Combined sources5
Helixi403 – 405Combined sources3
Helixi408 – 412Combined sources5
Helixi418 – 437Combined sources20
Helixi439 – 441Combined sources3
Beta strandi444 – 447Combined sources4
Helixi451 – 465Combined sources15
Helixi474 – 480Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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

CDDicd00401. SAHH. 1 hit.
Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00563. AdoHcyase. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP9WGV3. 1 interactor.
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.
BioCyciMTBH37RV:G185E-7522-MONOMER.

Family and domain databases

CDDicd00401. SAHH. 1 hit.
Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00563. AdoHcyase. 1 hit.
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...

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: November 30, 2016
This is version 22 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.