Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A7ZI51

- BETB_ECO24

UniProt

A7ZI51 - BETB_ECO24

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

NAD/NADP-dependent betaine aldehyde dehydrogenase

Gene

betB

Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Status
Reviewed - 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 bindingi26 – 261Potassium 1UniRule annotation
Metal bindingi27 – 271Potassium 1; via carbonyl oxygenUniRule annotation
Metal bindingi93 – 931Potassium 1UniRule annotation
Active sitei162 – 1621Charge relay systemUniRule annotation
Metal bindingi180 – 1801Potassium 1; via carbonyl oxygenUniRule annotation
Binding sitei209 – 2091NAD/NADP; via amide nitrogenUniRule annotation
Metal bindingi246 – 2461Potassium 2; via carbonyl oxygenUniRule annotation
Sitei248 – 2481Seems to be a necessary countercharge to the potassium cationsUniRule annotation
Active sitei252 – 2521Proton acceptorUniRule annotation
Binding sitei286 – 2861NAD/NADPUniRule annotation
Binding sitei387 – 3871NAD/NADPUniRule annotation
Metal bindingi457 – 4571Potassium 2; via carbonyl oxygenUniRule annotation
Metal bindingi460 – 4601Potassium 2; via carbonyl oxygenUniRule annotation
Active sitei464 – 4641Charge relay systemUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi150 – 1534NAD/NADPUniRule annotation
Nucleotide bindingi176 – 1794NAD/NADPUniRule annotation
Nucleotide bindingi229 – 2346NAD/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

BioCyciECOL331111:GH7P-325-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:EcE24377A_0327
OrganismiEscherichia coli O139:H28 (strain E24377A / ETEC)
Taxonomic identifieri331111 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001122: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490NAD/NADP-dependent betaine aldehyde dehydrogenasePRO_1000062268Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei286 – 2861Cysteine sulfenic acid (-SOH)UniRule annotation

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Dimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi331111.EcE24377A_0327.

Structurei

3D structure databases

ProteinModelPortaliA7ZI51.
SMRiA7ZI51. Positions 2-490.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
KOiK00130.
OMAiRANGTHL.
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.

A7ZI51-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRMAEQQLY IHGGYTSATS GRTFETINPA NGNVLATVQA AGREDVDRAV
60 70 80 90 100
KSAQQGQKIW AAMTAMERSR ILRRAVDILR ERNDELAKLE TLDTGKAYSE
110 120 130 140 150
TSTVDIVTGA DVLEYYAGLI PSLEGSQIPL RETSFVYTRR EPLGVVAGIG
160 170 180 190 200
AWNYPIQIAL WKSAPALAAG NAMIFKPSEV TPLTALKLAE IYSEAGLPDG
210 220 230 240 250
VFNVLPGVGA ETGQYLTEHP GIAKVSFTGG VASGKKVMAN SAASSLKEVT
260 270 280 290 300
MELGGKSPLI VFDDADLDLA ADIAMMANFF SSGQVCTNGT RVFVPAKCKA
310 320 330 340 350
AFEQKILARV ERIRAGDVFD PQTNFGPLVS FPHRDNVLRY IVKGKEEGAR
360 370 380 390 400
VLCGGDVLKG DGLDNGAWVA PTVFTDCSDE MTIVREEIFG PVMSILTYES
410 420 430 440 450
EEEVIRRAND TDYGLAAGIV TADLNRAHRV IHQLEAGICW INTWGESPAE
460 470 480 490
MPVGGYKHSG IGRENGVMTL QSYTQVKSIQ VEMAKFQSIF
Length:490
Mass (Da):52,933
Last modified:October 23, 2007 - v1
Checksum:i7FBCC44C933FBB2D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000800 Genomic DNA. Translation: ABV18550.1.
RefSeqiYP_001461480.1. NC_009801.1.

Genome annotation databases

EnsemblBacteriaiABV18550; ABV18550; EcE24377A_0327.
GeneIDi5588779.
KEGGiecw:EcE24377A_0327.
PATRICi18289926. VBIEscCol31211_0644.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000800 Genomic DNA. Translation: ABV18550.1 .
RefSeqi YP_001461480.1. NC_009801.1.

3D structure databases

ProteinModelPortali A7ZI51.
SMRi A7ZI51. Positions 2-490.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 331111.EcE24377A_0327.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV18550 ; ABV18550 ; EcE24377A_0327 .
GeneIDi 5588779.
KEGGi ecw:EcE24377A_0327.
PATRICi 18289926. VBIEscCol31211_0644.

Phylogenomic databases

eggNOGi COG1012.
HOGENOMi HOG000271505.
KOi K00130.
OMAi RANGTHL.
OrthoDBi EOG6BS8QW.

Enzyme and pathway databases

UniPathwayi UPA00529 ; UER00386 .
BioCyci ECOL331111:GH7P-325-MONOMER.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPi MF_00804. BADH.
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.
IPR011264. BADH.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR01804. BADH. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
    Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
    J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: E24377A / ETEC.

Entry informationi

Entry nameiBETB_ECO24
AccessioniPrimary (citable) accession number: A7ZI51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: November 26, 2014
This is version 53 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

Documents

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

External Data

Dasty 3