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P17202

- BADH_SPIOL

UniProt

P17202 - BADH_SPIOL

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Protein
Betaine aldehyde dehydrogenase, chloroplastic
Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei159 – 1591Transition state stabilizer By similarity
Active sitei257 – 2571Proton acceptor By similarity
Active sitei291 – 2911Nucleophile By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi235 – 2406NAD By similarity

GO - Molecular functioni

  1. betaine-aldehyde dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycine betaine biosynthetic process from choline Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00529; UER00386.

Names & Taxonomyi

Protein namesi
Recommended name:
Betaine aldehyde dehydrogenase, chloroplastic (EC:1.2.1.8)
Short name:
BADH
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 77Chloroplast Reviewed prediction
Chaini8 – 497490Betaine aldehyde dehydrogenase, chloroplastic
PRO_0000007182Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Blocked amino end (Arg)

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123
Beta strandi15 – 173
Beta strandi24 – 285
Turni30 – 323
Beta strandi35 – 406
Helixi44 – 5916
Turni61 – 633
Beta strandi64 – 663
Helixi68 – 8417
Helixi86 – 9712
Helixi101 – 12525
Turni126 – 1305
Beta strandi140 – 1489
Beta strandi150 – 1556
Beta strandi158 – 1603
Helixi161 – 17515
Beta strandi178 – 1825
Helixi189 – 20113
Beta strandi207 – 2104
Helixi215 – 22410
Beta strandi230 – 2356
Helixi237 – 24812
Turni249 – 2513
Beta strandi254 – 2574
Beta strandi263 – 2664
Beta strandi268 – 2703
Helixi272 – 28413
Helixi285 – 2884
Beta strandi296 – 3005
Helixi301 – 31616
Helixi336 – 35217
Beta strandi368 – 3703
Beta strandi375 – 3795
Helixi385 – 3884
Beta strandi393 – 40311
Helixi404 – 4118
Beta strandi418 – 4236
Helixi427 – 43610
Beta strandi439 – 4468
Helixi460 – 4623
Turni469 – 4713
Helixi472 – 4765
Beta strandi477 – 4859

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A0MX-ray2.30A/B/C/D1-496[»]
ProteinModelPortaliP17202.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17202-1 [UniParc]FASTAAdd to Basket

« Hide

MAFPIPARQL FIDGEWREPI KKNRIPVINP STEEIIGDIP AATAEDVEVA    50
VVAARRAFRR NNWSATSGAH RATYLRAIAA KITEKKDHFV KLETIDSGKP 100
FDEAVLDIDD VASCFEYFAG QAEALDGKQK APVTLPMERF KSHVLRQPLG 150
VVGLISPWNY PLLMATWKIA PALAAGCTAV LKPSELASVT CLEFGEVCNE 200
VGLPPGVLNI LTGLGPDAGA PLVSHPDVDK IAFTGSSATG SKVMASAAQL 250
VKPVTLELGG KSPIVVFEDV DIDKVVEWTI FGCFWTNGQI CSATSRLLVH 300
ESIAAEFVDK LVKWTKNIKI SDPFEEGCRL GPVISKGQYD KIMKFISTAK 350
SEGATILYGG SRPEHLKKGY YIEPTIVTDI STSMQIWKEE VFGPVLCVKT 400
FSSEDEAIAL ANDTEYGLAA AVFSNDLERC ERITKALEVG AVWVNCSQPC 450
FVQAPWGGIK RSGFGRELGE WGIQNYLNIK QVTQDISDEP WGWYKSP 497
Length:497
Mass (Da):54,270
Last modified:November 1, 1990 - v1
Checksum:i55088240E635B22F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti424 – 4241S → F in AAB41696. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31480 mRNA. Translation: AAA34025.1.
U69142 Genomic DNA. Translation: AAB41696.1.
PIRiA35994.
T51173.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31480 mRNA. Translation: AAA34025.1 .
U69142 Genomic DNA. Translation: AAB41696.1 .
PIRi A35994.
T51173.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4A0M X-ray 2.30 A/B/C/D 1-496 [» ]
ProteinModelPortali P17202.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00529 ; UER00386 .

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiBADH_SPIOL
AccessioniPrimary (citable) accession number: P17202
Secondary accession number(s): P93555
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 11, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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

External Data

Dasty 3

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