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Protein

Betaine aldehyde dehydrogenase, chloroplastic

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: betaine biosynthesis via choline pathway

This protein is involved in step 1 of the subpathway that synthesizes betaine from betaine aldehyde.
Proteins known to be involved in this subpathway in this organism are:
  1. Betaine aldehyde dehydrogenase, chloroplastic
This subpathway is part of the pathway betaine biosynthesis via choline pathway, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes betaine from betaine aldehyde, the pathway betaine biosynthesis via choline pathway and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei159Transition state stabilizerBy similarity1
Active sitei257Proton acceptorPROSITE-ProRule annotation1
Active sitei291NucleophilePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi235 – 240NADBy similarity6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.2.1.8. 5812.
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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 7ChloroplastSequence analysis7
ChainiPRO_00000071828 – 497Betaine aldehyde dehydrogenase, chloroplasticAdd BLAST490

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei8Blocked amino end (Arg)1

Proteomic databases

PRIDEiP17202.

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1497
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 12Combined sources3
Beta strandi15 – 17Combined sources3
Beta strandi24 – 28Combined sources5
Turni30 – 32Combined sources3
Beta strandi35 – 40Combined sources6
Helixi44 – 59Combined sources16
Beta strandi60 – 63Combined sources4
Beta strandi64 – 66Combined sources3
Helixi68 – 84Combined sources17
Helixi86 – 97Combined sources12
Helixi101 – 126Combined sources26
Turni127 – 130Combined sources4
Beta strandi131 – 133Combined sources3
Beta strandi140 – 148Combined sources9
Beta strandi150 – 155Combined sources6
Beta strandi158 – 160Combined sources3
Helixi161 – 175Combined sources15
Beta strandi178 – 182Combined sources5
Helixi185 – 187Combined sources3
Helixi189 – 201Combined sources13
Beta strandi207 – 210Combined sources4
Helixi215 – 224Combined sources10
Beta strandi230 – 235Combined sources6
Helixi237 – 249Combined sources13
Beta strandi254 – 257Combined sources4
Beta strandi262 – 266Combined sources5
Beta strandi268 – 270Combined sources3
Helixi272 – 284Combined sources13
Helixi285 – 288Combined sources4
Beta strandi294 – 300Combined sources7
Helixi301 – 316Combined sources16
Helixi336 – 352Combined sources17
Beta strandi355 – 358Combined sources4
Beta strandi368 – 370Combined sources3
Beta strandi375 – 379Combined sources5
Helixi385 – 388Combined sources4
Beta strandi393 – 403Combined sources11
Helixi404 – 412Combined sources9
Beta strandi418 – 423Combined sources6
Helixi427 – 436Combined sources10
Beta strandi439 – 446Combined sources8
Helixi460 – 462Combined sources3
Helixi469 – 476Combined sources8
Beta strandi477 – 485Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4A0MX-ray2.30A/B/C/D1-496[»]
4V37X-ray2.10A/B/C/D1-497[»]
4V3FX-ray2.00A/B/C/D1-497[»]
5A2DX-ray1.98A/B/C/D1-497[»]
ProteinModelPortaliP17202.
SMRiP17202.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

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.
IPR012394. Aldehyde_DH_NAD(P).
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF036492. ALDH. 1 hit.
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

        10         20         30         40         50
MAFPIPARQL FIDGEWREPI KKNRIPVINP STEEIIGDIP AATAEDVEVA
60 70 80 90 100
VVAARRAFRR NNWSATSGAH RATYLRAIAA KITEKKDHFV KLETIDSGKP
110 120 130 140 150
FDEAVLDIDD VASCFEYFAG QAEALDGKQK APVTLPMERF KSHVLRQPLG
160 170 180 190 200
VVGLISPWNY PLLMATWKIA PALAAGCTAV LKPSELASVT CLEFGEVCNE
210 220 230 240 250
VGLPPGVLNI LTGLGPDAGA PLVSHPDVDK IAFTGSSATG SKVMASAAQL
260 270 280 290 300
VKPVTLELGG KSPIVVFEDV DIDKVVEWTI FGCFWTNGQI CSATSRLLVH
310 320 330 340 350
ESIAAEFVDK LVKWTKNIKI SDPFEEGCRL GPVISKGQYD KIMKFISTAK
360 370 380 390 400
SEGATILYGG SRPEHLKKGY YIEPTIVTDI STSMQIWKEE VFGPVLCVKT
410 420 430 440 450
FSSEDEAIAL ANDTEYGLAA AVFSNDLERC ERITKALEVG AVWVNCSQPC
460 470 480 490
FVQAPWGGIK RSGFGRELGE WGIQNYLNIK QVTQDISDEP WGWYKSP
Length:497
Mass (Da):54,270
Last modified:November 1, 1990 - v1
Checksum:i55088240E635B22F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti424S → F in AAB41696 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31480 mRNA. Translation: AAA34025.1.
U69142 Genomic DNA. Translation: AAB41696.1.
PIRiA35994.
T51173.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31480 mRNA. Translation: AAA34025.1.
U69142 Genomic DNA. Translation: AAB41696.1.
PIRiA35994.
T51173.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4A0MX-ray2.30A/B/C/D1-496[»]
4V37X-ray2.10A/B/C/D1-497[»]
4V3FX-ray2.00A/B/C/D1-497[»]
5A2DX-ray1.98A/B/C/D1-497[»]
ProteinModelPortaliP17202.
SMRiP17202.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP17202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00529; UER00386.
BRENDAi1.2.1.8. 5812.

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.
IPR012394. Aldehyde_DH_NAD(P).
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF036492. ALDH. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 99 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

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.