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Protein

Adenosylhomocysteinase

Gene

SAHH

Organism
Lupinus luteus (European yellow lupine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.By similarity

Catalytic activityi

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

Cofactori

NAD+By similarityNote: Binds 1 NAD+ per subunit.By similarity

Pathwayi: L-homocysteine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-homocysteine from S-adenosyl-L-homocysteine.
Proteins known to be involved in this subpathway in this organism are:
  1. Adenosylhomocysteinase (SAHH)
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 sitei64SubstrateBy similarity1
Binding sitei139SubstrateBy similarity1
Binding sitei205SubstrateBy similarity1
Binding sitei235SubstrateBy similarity1
Binding sitei239SubstrateBy similarity1
Binding sitei240NADBy similarity1
Binding sitei292NADBy similarity1
Binding sitei327NADBy similarity1
Binding sitei397NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi206 – 208NADBy similarity3
Nucleotide bindingi269 – 274NADBy similarity6
Nucleotide bindingi348 – 350NADBy similarity3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processOne-carbon metabolism
LigandNAD

Enzyme and pathway databases

BRENDAi3.3.1.1. 3093.
UniPathwayiUPA00314; UER00076.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosylhomocysteinase (EC:3.3.1.1)
Short name:
AdoHcyase
Alternative name(s):
S-adenosyl-L-homocysteine hydrolase
Gene namesi
Name:SAHH
Synonyms:SHH
OrganismiLupinus luteus (European yellow lupine)
Taxonomic identifieri3873 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeGenisteaeLupinus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001169231 – 485AdenosylhomocysteinaseAdd BLAST485

Proteomic databases

PRIDEiQ9SP37.

Structurei

Secondary structure

1485
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 17Combined sources5
Helixi19 – 21Combined sources3
Helixi22 – 34Combined sources13
Helixi37 – 46Combined sources10
Helixi47 – 49Combined sources3
Turni51 – 54Combined sources4
Beta strandi56 – 61Combined sources6
Helixi65 – 76Combined sources12
Beta strandi80 – 84Combined sources5
Turni88 – 90Combined sources3
Helixi93 – 102Combined sources10
Beta strandi105 – 108Combined sources4
Helixi114 – 125Combined sources12
Beta strandi134 – 141Combined sources8
Helixi142 – 160Combined sources19
Helixi166 – 168Combined sources3
Helixi172 – 185Combined sources14
Helixi191 – 198Combined sources8
Beta strandi201 – 204Combined sources4
Helixi207 – 218Combined sources12
Beta strandi226 – 228Combined sources3
Helixi233 – 236Combined sources4
Helixi239 – 256Combined sources18
Beta strandi264 – 268Combined sources5
Helixi272 – 283Combined sources12
Beta strandi287 – 291Combined sources5
Helixi295 – 303Combined sources9
Helixi311 – 313Combined sources3
Turni314 – 317Combined sources4
Beta strandi319 – 323Combined sources5
Helixi333 – 336Combined sources4
Beta strandi343 – 350Combined sources8
Turni351 – 354Combined sources4
Helixi357 – 361Combined sources5
Beta strandi367 – 372Combined sources6
Beta strandi375 – 379Combined sources5
Turni381 – 383Combined sources3
Beta strandi386 – 390Combined sources5
Helixi391 – 393Combined sources3
Helixi396 – 400Combined sources5
Helixi406 – 425Combined sources20
Turni426 – 429Combined sources4
Beta strandi434 – 437Combined sources4
Helixi441 – 452Combined sources12
Helixi453 – 455Combined sources3
Helixi464 – 469Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ONDX-ray1.17A/B1-485[»]
3ONEX-ray1.35A/B1-485[»]
3ONFX-ray2.00A/B1-485[»]
ProteinModelPortaliQ9SP37.
SMRiQ9SP37.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9SP37.

Family & Domainsi

Sequence similaritiesi

Belongs to the adenosylhomocysteinase family.Curated

Family and domain databases

CDDicd00401. SAHH. 1 hit.
HAMAPiMF_00563. AdoHcyase. 1 hit.
InterProiView protein in InterPro
IPR034373. Adenosylhomocysteinase.
IPR000043. Adenosylhomocysteinase-like.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR036291. NAD(P)-bd_dom_sf.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
PANTHERiPTHR23420. PTHR23420. 1 hit.
PfamiView protein in Pfam
PF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
PIRSFiPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTiView protein in SMART
SM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00936. ahcY. 1 hit.
PROSITEiView protein in PROSITE
PS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9SP37-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLVEKTTS GREYKVKDMS QADFGRLEIE LAEVEMPGLM ASRSEFGPSQ
60 70 80 90 100
PFKGAKITGS LHMTIQTAVL IETLTALGAE VRWCSCNIFS TQDHAAAAIA
110 120 130 140 150
RDSAAVFAWK GETLQEYWWC TERALDWGPG GGPDLIVDDG GDTTLLIHEG
160 170 180 190 200
VKAEEIYEKS GQFPDPDSTD NAEFKIVLSI IKEGLKTDPK RYHKMKDRVV
210 220 230 240 250
GVSEETTTGV KRLYQMQANG TLLFPAINVN DSVTKSKFDN LYGCRHSLPD
260 270 280 290 300
GLMRATDVMI AGKVAVVAGY GDVGKGCAAA LKQAGARVIV TEIDPICALQ
310 320 330 340 350
ATMEGLQVLT LEDVVSEADI FVTTTGNKDI IMLDHMKKMK NNAIVCNIGH
360 370 380 390 400
FDNEIDMLGL ETHPGVKRIT IKPQTDRWVF PETNTGIIIL AEGRLMNLGC
410 420 430 440 450
ATGHPSFVMS CSFTNQVIAQ LELWNEKSSG KYEKKVYVLP KHLDEKVAAL
460 470 480
HLEKLGAKLT KLSKDQADYI SVPVEGPYKP FHYRY
Length:485
Mass (Da):53,326
Last modified:May 1, 2000 - v1
Checksum:i42F8FA6C58A42B19
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF185635 mRNA. Translation: AAD56048.1.

Similar proteinsi

Entry informationi

Entry nameiSAHH_LUPLU
AccessioniPrimary (citable) accession number: Q9SP37
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: May 1, 2000
Last modified: October 25, 2017
This is version 85 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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