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P17202 (BADH_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Betaine aldehyde dehydrogenase, chloroplastic

Short name=BADH
EC=1.2.1.8
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Betaine aldehyde + NAD+ + H2O = betaine + NADH.

Pathway

Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1.

Subunit structure

Homodimer.

Subcellular location

Plastidchloroplast.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processglycine betaine biosynthetic process from choline

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbetaine-aldehyde dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 77Chloroplast Potential
Chain8 – 497490Betaine aldehyde dehydrogenase, chloroplastic
PRO_0000007182

Regions

Nucleotide binding235 – 2406NAD By similarity

Sites

Active site2571Proton acceptor By similarity
Active site2911Nucleophile By similarity
Site1591Transition state stabilizer By similarity

Amino acid modifications

Modified residue81Blocked amino end (Arg)

Experimental info

Sequence conflict4241S → F in AAB41696. Ref.2

Secondary structure

.............................................................................. 497
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17202 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 55088240E635B22F

FASTA49754,270
        10         20         30         40         50         60 
MAFPIPARQL FIDGEWREPI KKNRIPVINP STEEIIGDIP AATAEDVEVA VVAARRAFRR 

        70         80         90        100        110        120 
NNWSATSGAH RATYLRAIAA KITEKKDHFV KLETIDSGKP FDEAVLDIDD VASCFEYFAG 

       130        140        150        160        170        180 
QAEALDGKQK APVTLPMERF KSHVLRQPLG VVGLISPWNY PLLMATWKIA PALAAGCTAV 

       190        200        210        220        230        240 
LKPSELASVT CLEFGEVCNE VGLPPGVLNI LTGLGPDAGA PLVSHPDVDK IAFTGSSATG 

       250        260        270        280        290        300 
SKVMASAAQL VKPVTLELGG KSPIVVFEDV DIDKVVEWTI FGCFWTNGQI CSATSRLLVH 

       310        320        330        340        350        360 
ESIAAEFVDK LVKWTKNIKI SDPFEEGCRL GPVISKGQYD KIMKFISTAK SEGATILYGG 

       370        380        390        400        410        420 
SRPEHLKKGY YIEPTIVTDI STSMQIWKEE VFGPVLCVKT FSSEDEAIAL ANDTEYGLAA 

       430        440        450        460        470        480 
AVFSNDLERC ERITKALEVG AVWVNCSQPC FVQAPWGGIK RSGFGRELGE WGIQNYLNIK 

       490 
QVTQDISDEP WGWYKSP 

« Hide

References

[1]"Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought."
Weretilnyk E.A., Hanson A.D.
Proc. Natl. Acad. Sci. U.S.A. 87:2745-2749(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Savoy hybrid 612.
[2]Shu W., Ai W., Chen S.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31480 mRNA. Translation: AAA34025.1.
U69142 Genomic DNA. Translation: AAB41696.1.
PIRA35994.
T51173.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4A0MX-ray2.30A/B/C/D1-496[»]
ProteinModelPortalP17202.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00529; UER00386.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBADH_SPIOL
AccessionPrimary (citable) accession number: P17202
Secondary accession number(s): P93555
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: February 19, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways