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Protein

Adenosylhomocysteinase

Gene

ahcY

Organism
Brucella abortus (strain 2308)
Status
Reviewed-Annotation score: Annotation score: 3 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 annotationNote: Binds 1 NAD+ per subunit.UniRule annotation

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)
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 sitei57SubstrateUniRule annotation1
Binding sitei132SubstrateUniRule annotation1
Binding sitei192SubstrateUniRule annotation1
Binding sitei222SubstrateUniRule annotation1
Binding sitei226SubstrateUniRule annotation1
Binding sitei227NADUniRule annotation1
Binding sitei279NADUniRule annotation1
Binding sitei314NADUniRule annotation1
Binding sitei380NADUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi193 – 195NADUniRule annotation3
Nucleotide bindingi256 – 261NADUniRule annotation6
Nucleotide bindingi335 – 337NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

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
Ordered Locus Names:BAB1_2099
OrganismiBrucella abortus (strain 2308)
Taxonomic identifieri359391 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000002719 Componenti: Chromosome I

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000247111 – 466AdenosylhomocysteinaseAdd BLAST466

Proteomic databases

PRIDEiQ2YQX8.

Structurei

Secondary structure

1466
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 10Combined sources3
Helixi12 – 14Combined sources3
Helixi15 – 26Combined sources12
Helixi30 – 39Combined sources10
Turni40 – 42Combined sources3
Turni44 – 47Combined sources4
Beta strandi49 – 54Combined sources6
Helixi58 – 69Combined sources12
Beta strandi73 – 77Combined sources5
Helixi86 – 94Combined sources9
Beta strandi99 – 101Combined sources3
Helixi107 – 116Combined sources10
Beta strandi127 – 134Combined sources8
Helixi135 – 147Combined sources13
Beta strandi153 – 155Combined sources3
Helixi159 – 174Combined sources16
Helixi178 – 185Combined sources8
Beta strandi188 – 191Combined sources4
Helixi194 – 206Combined sources13
Beta strandi213 – 215Combined sources3
Helixi220 – 223Combined sources4
Helixi226 – 243Combined sources18
Beta strandi251 – 255Combined sources5
Helixi259 – 270Combined sources12
Beta strandi274 – 278Combined sources5
Helixi282 – 290Combined sources9
Helixi298 – 301Combined sources4
Helixi302 – 304Combined sources3
Beta strandi306 – 310Combined sources5
Beta strandi313 – 318Combined sources6
Helixi320 – 325Combined sources6
Beta strandi330 – 334Combined sources5
Beta strandi336 – 338Combined sources3
Turni339 – 341Combined sources3
Helixi345 – 347Combined sources3
Beta strandi350 – 356Combined sources7
Beta strandi359 – 363Combined sources5
Beta strandi369 – 373Combined sources5
Helixi374 – 376Combined sources3
Helixi379 – 383Combined sources5
Helixi389 – 408Combined sources20
Helixi410 – 412Combined sources3
Beta strandi415 – 418Combined sources4
Helixi422 – 432Combined sources11
Helixi434 – 436Combined sources3
Helixi445 – 451Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3N58X-ray2.39A/B/C/D8-466[»]
ProteinModelPortaliQ2YQX8.
SMRiQ2YQX8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2YQX8.

Family & Domainsi

Sequence similaritiesi

Belongs to the adenosylhomocysteinase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000227986.
KOiK01251.
OMAiKYGCRES.

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.

Q2YQX8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTASQDFVVK DISLADWGRK ELDIAETEMP GLMAAREEFG KSQPLKGARI
60 70 80 90 100
SGSLHMTIQT AVLIETLKVL GAEVRWASCN IFSTQDHAAA AIAATGTPVF
110 120 130 140 150
AVKGETLEEY WTYTDQIFQW PDGEPSNMIL DDGGDATMYI LIGARAEAGE
160 170 180 190 200
DVLSNPQSEE EEVLFAQIKK RMAATPGFFT KQRAAIKGVT EETTTGVNRL
210 220 230 240 250
YQLQKKGLLP FPAINVNDSV TKSKFDNKYG CKESLVDGIR RGTDVMMAGK
260 270 280 290 300
VAVVCGYGDV GKGSAQSLAG AGARVKVTEV DPICALQAAM DGFEVVTLDD
310 320 330 340 350
AASTADIVVT TTGNKDVITI DHMRKMKDMC IVGNIGHFDN EIQVAALRNL
360 370 380 390 400
KWTNVKPQVD LIEFPDGKRL ILLSEGRLLN LGNATGHPSF VMSASFTNQV
410 420 430 440 450
LGQIELFTRT DAYKNEVYVL PKHLDEKVAR LHLDKLGAKL TVLSEEQAAY
460
IGVTPQGPFK SEHYRY
Length:466
Mass (Da):50,791
Last modified:February 7, 2006 - v1
Checksum:i6AB3B4B1C2F0BE41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM040264 Genomic DNA. Translation: CAJ12055.1.
RefSeqiWP_002965162.1. NZ_KN046823.1.

Genome annotation databases

EnsemblBacteriaiCAJ12055; CAJ12055; BAB1_2099.
GeneIDi3788612.
KEGGibmf:BAB1_2099.
PATRICi17847299. VBIBruMel86222_2185.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM040264 Genomic DNA. Translation: CAJ12055.1.
RefSeqiWP_002965162.1. NZ_KN046823.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3N58X-ray2.39A/B/C/D8-466[»]
ProteinModelPortaliQ2YQX8.
SMRiQ2YQX8.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ2YQX8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAJ12055; CAJ12055; BAB1_2099.
GeneIDi3788612.
KEGGibmf:BAB1_2099.
PATRICi17847299. VBIBruMel86222_2185.

Phylogenomic databases

HOGENOMiHOG000227986.
KOiK01251.
OMAiKYGCRES.

Enzyme and pathway databases

UniPathwayiUPA00314; UER00076.

Miscellaneous databases

EvolutionaryTraceiQ2YQX8.

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_BRUA2
AccessioniPrimary (citable) accession number: Q2YQX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 7, 2006
Last modified: November 30, 2016
This is version 80 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. Brucella abortus strain 2308
    Brucella abortus (strain 2308): 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.