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Protein

NAD/NADP-dependent betaine aldehyde dehydrogenase

Gene

betB

Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid.UniRule annotation

Catalytic activityi

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

Cofactori

K(+)UniRule annotationNote: Binds 2 potassium ions per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi23 – 231Potassium 1UniRule annotation
Metal bindingi90 – 901Potassium 1UniRule annotation
Active sitei159 – 1591Charge relay systemUniRule annotation
Metal bindingi241 – 2411Potassium 2; via carbonyl oxygenUniRule annotation
Active sitei247 – 2471Proton acceptorUniRule annotation
Binding sitei281 – 2811NAD/NADPUniRule annotation
Binding sitei382 – 3821NAD/NADPUniRule annotation
Metal bindingi452 – 4521Potassium 2; via carbonyl oxygenUniRule annotation
Metal bindingi455 – 4551Potassium 2; via carbonyl oxygenUniRule annotation
Active sitei459 – 4591Charge relay systemUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi147 – 1504NAD/NADPUniRule annotation
Nucleotide bindingi173 – 1764NAD/NADPUniRule annotation
Nucleotide bindingi225 – 2306NAD/NADPUniRule annotation

GO - Molecular functioni

  1. betaine-aldehyde dehydrogenase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, NADP, Potassium

Enzyme and pathway databases

BioCyciVPAR223926:GHK4-4353-MONOMER.
UniPathwayiUPA00529; UER00386.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD/NADP-dependent betaine aldehyde dehydrogenaseUniRule annotation (EC:1.2.1.8UniRule annotation)
Short name:
BADHUniRule annotation
Gene namesi
Name:betBUniRule annotation
Ordered Locus Names:VPA1113
OrganismiVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Taxonomic identifieri223926 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000002493 Componenti: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486NAD/NADP-dependent betaine aldehyde dehydrogenasePRO_0000056555Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei281 – 2811Cysteine sulfenic acid (-SOH)UniRule annotation

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Dimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi223926.VPA1113.

Structurei

3D structure databases

ProteinModelPortaliQ87H52.
SMRiQ87H52. Positions 5-485.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
KOiK00130.
OMAiHVYQNIA.
OrthoDBiEOG6BS8QW.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPiMF_00804. BADH.
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.
IPR011264. BADH.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01804. BADH. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q87H52-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMKTHYIDG AMYIGCSEEH FTTYNPANGE PLANIKQANQ SDMEAAIESA
60 70 80 90 100
KRGFEVWSAM TAIERSRILN KAVAILRERN DELAALEVAD TGKPIQEAIA
110 120 130 140 150
VDITTGADVI EYYAGLAPSL QGEQQPLNEN QFFYTRREPL GICAGIGAWN
160 170 180 190 200
YPIQIAMWKS APALAAGNAM IFKPSEETPL TALKLAEIYS EAGLPDGVFN
210 220 230 240 250
VVQGDYRVGQ MLTAHPDIAK VSFTGESGTG KVVMGDSAKT LKQVTMELGG
260 270 280 290 300
KSPLIVFDDA KLDDAVSAAM VANFYTQGEV CTNGTRVFVH ESIYDDFVAQ
310 320 330 340 350
LKTRTEKLVV GDPLDENTQI GALISKEHES KVLSAIESAK ASGATLLTGG
360 370 380 390 400
YKVTDNGLQN GNFVAPTVFI DCDDSMSHVQ QEIFGPVMSV LKFSEEAEVI
410 420 430 440 450
ERANDTDYGL AAGVFTQNLS RAHRVIHKIQ AGICWVNAWG DSPAEMPVGG
460 470 480
YKQSGIGREN GVETLKHYTQ TKSVLVQLSD FESPYA
Length:486
Mass (Da):52,618
Last modified:June 1, 2003 - v1
Checksum:i1ECBF4B227E4C265
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000032 Genomic DNA. Translation: BAC62456.1.
RefSeqiNP_800623.1. NC_004605.1.

Genome annotation databases

EnsemblBacteriaiBAC62456; BAC62456; BAC62456.
GeneIDi1191809.
KEGGivpa:VPA1113.
PATRICi20146625. VBIVibPar50997_4039.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000032 Genomic DNA. Translation: BAC62456.1.
RefSeqiNP_800623.1. NC_004605.1.

3D structure databases

ProteinModelPortaliQ87H52.
SMRiQ87H52. Positions 5-485.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi223926.VPA1113.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC62456; BAC62456; BAC62456.
GeneIDi1191809.
KEGGivpa:VPA1113.
PATRICi20146625. VBIVibPar50997_4039.

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
KOiK00130.
OMAiHVYQNIA.
OrthoDBiEOG6BS8QW.

Enzyme and pathway databases

UniPathwayiUPA00529; UER00386.
BioCyciVPAR223926:GHK4-4353-MONOMER.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPiMF_00804. BADH.
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.
IPR011264. BADH.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01804. BADH. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
    Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
    Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RIMD 2210633.

Entry informationi

Entry nameiBETB_VIBPA
AccessioniPrimary (citable) accession number: Q87H52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: June 1, 2003
Last modified: January 7, 2015
This is version 78 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.