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Protein

Adenosylhomocysteinase

Gene

ahcY

Organism
Burkholderia pseudomallei (strain 1710b)
Status
Reviewed-Annotation score: Annotation score: 4 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+Note: Binds 1 NAD+ per subunit.

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 sitei64Substrate1
Binding sitei139Substrate1
Binding sitei199Substrate1
Binding sitei229Substrate1
Binding sitei233Substrate1
Binding sitei234NADUniRule annotation1
Binding sitei286NADUniRule annotation2 Publications1
Binding sitei321NADUniRule annotation2 Publications1
Binding sitei387NADUniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi200 – 202NADUniRule annotation3
Nucleotide bindingi263 – 268NADUniRule annotation6
Nucleotide bindingi266 – 267NADUniRule annotation2 Publications2
Nucleotide bindingi342 – 344NADUniRule annotation3
Nucleotide bindingi342 – 343NADUniRule annotation2 Publications2

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:BURPS1710b_0057
OrganismiBurkholderia pseudomallei (strain 1710b)
Taxonomic identifieri320372 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
Proteomesi
  • UP000002700 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_10000247181 – 473AdenosylhomocysteinaseAdd BLAST473

Structurei

Secondary structure

1473
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 21Combined sources3
Helixi22 – 32Combined sources11
Helixi33 – 35Combined sources3
Helixi37 – 45Combined sources9
Turni46 – 49Combined sources4
Turni51 – 54Combined sources4
Beta strandi56 – 61Combined sources6
Helixi65 – 76Combined sources12
Beta strandi80 – 84Combined sources5
Beta strandi86 – 89Combined sources4
Helixi93 – 101Combined sources9
Helixi114 – 123Combined sources10
Beta strandi135 – 141Combined sources7
Helixi142 – 155Combined sources14
Helixi157 – 160Combined sources4
Helixi166 – 179Combined sources14
Turni183 – 186Combined sources4
Helixi187 – 190Combined sources4
Beta strandi196 – 198Combined sources3
Helixi201 – 212Combined sources12
Beta strandi220 – 222Combined sources3
Helixi227 – 239Combined sources13
Helixi242 – 250Combined sources9
Beta strandi258 – 262Combined sources5
Helixi266 – 276Combined sources11
Turni277 – 279Combined sources3
Beta strandi281 – 285Combined sources5
Helixi289 – 296Combined sources8
Turni297 – 299Combined sources3
Helixi305 – 308Combined sources4
Turni309 – 311Combined sources3
Beta strandi313 – 317Combined sources5
Beta strandi319 – 322Combined sources4
Helixi327 – 332Combined sources6
Beta strandi337 – 341Combined sources5
Beta strandi343 – 346Combined sources4
Helixi352 – 354Combined sources3
Beta strandi357 – 363Combined sources7
Beta strandi366 – 370Combined sources5
Beta strandi376 – 380Combined sources5
Helixi381 – 383Combined sources3
Helixi386 – 389Combined sources4
Helixi396 – 416Combined sources21
Helixi417 – 419Combined sources3
Beta strandi422 – 426Combined sources5
Helixi429 – 440Combined sources12
Turni441 – 444Combined sources4
Helixi452 – 458Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3D64X-ray2.30A/B1-473[»]
3GLQX-ray2.30A/B1-473[»]
ProteinModelPortaliQ3JY79.
SMRiQ3JY79.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3JY79.

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.

Q3JY79-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAAVIDSHS AQDYVVADIA LAGWGRKELN IAETEMPGLV QIRDEYKAQQ
60 70 80 90 100
PLKGARIAGS LHMTIQTGVL IETLKALGAD VRWASCNIFS TQDHAAAAIV
110 120 130 140 150
EAGTPVFAFK GESLDEYWEF SHRIFEWPNG EFANMILDDG GDATLLLILG
160 170 180 190 200
SKAEKDRSVI ARPTNEEEVA LFKSIERHLE IDGSWYSKRL AHIKGVTEET
210 220 230 240 250
TTGVHRLYQM EKDGRLPFPA FNVNDSVTKS KFDNLYGCRE SLVDGIKRAT
260 270 280 290 300
DVMIAGKIAV VAGYGDVGKG CAQSLRGLGA TVWVTEIDPI CALQAAMEGY
310 320 330 340 350
RVVTMEYAAD KADIFVTATG NYHVINHDHM KAMRHNAIVC NIGHFDSEID
360 370 380 390 400
VASTRQYQWE NIKPQVDHII FPDGKRVILL AEGRLVNLGC ATGHPSFVMS
410 420 430 440 450
NSFTNQTLAQ IELFTRGGEY ANKVYVLPKH LDEKVARLHL ARIGAQLSEL
460 470
SDDQAAYIGV SKAGPFKPDH YRY
Length:473
Mass (Da):52,201
Last modified:November 8, 2005 - v1
Checksum:i7A40ECDD0A47B596
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000124 Genomic DNA. Translation: ABA47924.1.
RefSeqiWP_004198634.1. NC_007434.1.

Genome annotation databases

EnsemblBacteriaiABA47924; ABA47924; BURPS1710b_0057.
KEGGibpm:BURPS1710b_0057.
PATRICi19232326. VBIBurPse115837_0057.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000124 Genomic DNA. Translation: ABA47924.1.
RefSeqiWP_004198634.1. NC_007434.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3D64X-ray2.30A/B1-473[»]
3GLQX-ray2.30A/B1-473[»]
ProteinModelPortaliQ3JY79.
SMRiQ3JY79.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA47924; ABA47924; BURPS1710b_0057.
KEGGibpm:BURPS1710b_0057.
PATRICi19232326. VBIBurPse115837_0057.

Phylogenomic databases

HOGENOMiHOG000227986.
KOiK01251.
OMAiKYGCRES.

Enzyme and pathway databases

UniPathwayiUPA00314; UER00076.

Miscellaneous databases

EvolutionaryTraceiQ3JY79.

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_BURP1
AccessioniPrimary (citable) accession number: Q3JY79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 8, 2005
Last modified: November 30, 2016
This is version 86 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.