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Q9HTJ1

- BETB_PSEAE

UniProt

Q9HTJ1 - BETB_PSEAE

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Protein

NAD/NADP-dependent betaine aldehyde dehydrogenase

Gene

betB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid.1 PublicationUniRule annotation

Catalytic activityi

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

Cofactori

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi26 – 261Potassium 1
Metal bindingi27 – 271Potassium 1; via carbonyl oxygen
Metal bindingi93 – 931Potassium 1
Active sitei162 – 1621Charge relay system1 PublicationUniRule annotation
Metal bindingi180 – 1801Potassium 1; via carbonyl oxygen
Binding sitei209 – 2091NAD/NADP; via amide nitrogen
Metal bindingi246 – 2461Potassium 2; via carbonyl oxygen
Sitei248 – 2481Seems to be a necessary countercharge to the potassium cations
Active sitei252 – 2521Proton acceptor1 PublicationUniRule annotation
Binding sitei286 – 2861NAD/NADP
Binding sitei387 – 3871NAD/NADP
Metal bindingi457 – 4571Potassium 2; via carbonyl oxygen
Metal bindingi460 – 4601Potassium 2; via carbonyl oxygen
Active sitei464 – 4641Charge relay system1 PublicationUniRule annotation

Regions

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

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, Potassium

Enzyme and pathway databases

BRENDAi1.2.1.8. 5087.
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:PA5373
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA5373.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490NAD/NADP-dependent betaine aldehyde dehydrogenasePRO_0000056546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei286 – 2861Cysteine sulfenic acid (-SOH)1 PublicationUniRule annotation

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Dimer of dimers.3 PublicationsUniRule annotation

Protein-protein interaction databases

STRINGi208964.PA5373.

Structurei

Secondary structure

1
490
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 165Combined sources
Beta strandi19 – 213Combined sources
Beta strandi23 – 275Combined sources
Turni29 – 313Combined sources
Beta strandi34 – 396Combined sources
Helixi43 – 6220Combined sources
Helixi65 – 8117Combined sources
Helixi83 – 9412Combined sources
Helixi98 – 1014Combined sources
Turni102 – 1043Combined sources
Helixi105 – 11915Combined sources
Helixi120 – 1223Combined sources
Beta strandi125 – 1317Combined sources
Beta strandi134 – 1429Combined sources
Beta strandi144 – 1496Combined sources
Beta strandi152 – 1543Combined sources
Helixi155 – 16814Combined sources
Beta strandi172 – 1765Combined sources
Helixi183 – 19513Combined sources
Beta strandi201 – 2044Combined sources
Turni209 – 2113Combined sources
Helixi212 – 2187Combined sources
Beta strandi224 – 2296Combined sources
Helixi231 – 24515Combined sources
Beta strandi248 – 2525Combined sources
Beta strandi258 – 2614Combined sources
Helixi267 – 27913Combined sources
Helixi280 – 2834Combined sources
Beta strandi291 – 2955Combined sources
Helixi296 – 2983Combined sources
Helixi299 – 31113Combined sources
Helixi331 – 34616Combined sources
Beta strandi350 – 3534Combined sources
Turni360 – 3623Combined sources
Helixi363 – 3653Combined sources
Beta strandi372 – 3765Combined sources
Helixi382 – 3854Combined sources
Beta strandi390 – 39910Combined sources
Helixi401 – 4099Combined sources
Beta strandi415 – 4206Combined sources
Helixi424 – 43310Combined sources
Beta strandi437 – 4426Combined sources
Helixi457 – 4593Combined sources
Beta strandi460 – 4623Combined sources
Helixi466 – 4716Combined sources
Beta strandi474 – 4829Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WMEX-ray2.10A/B/C/D/E/F/G/H1-490[»]
2WOXX-ray2.30A/B/C/D2-490[»]
2XDRX-ray2.30A/B/C/D2-490[»]
3ZQAX-ray2.45A/B/C/D1-490[»]
ProteinModelPortaliQ9HTJ1.
SMRiQ9HTJ1. Positions 2-490.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HTJ1.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
InParanoidiQ9HTJ1.
KOiK00130.
OMAiCTDEMTI.
OrthoDBiEOG6BS8QW.
PhylomeDBiQ9HTJ1.

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.

Q9HTJ1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARFEEQKLY IGGRYVEASS GATFETINPA NGEVLAKVQR ASREDVERAV
60 70 80 90 100
QSAVEGQKVW AAMTAMQRSR ILRRAVDILR ERNDELAALE TLDTGKPLAE
110 120 130 140 150
TRSVDIVTGA DVLEYYAGLV PAIEGEQIPL RETSFVYTRR EPLGVVAGIG
160 170 180 190 200
AWNYPVQIAL WKSAPALAAG NAMIFKPSEV TPLTALKLAE IYTEAGVPDG
210 220 230 240 250
VFNVLTGSGR EVGQWLTEHP LIEKISFTGG TSTGKKVMAS ASSSSLKEVT
260 270 280 290 300
MELGGKSPLI IFPDADLDRA ADIAVMANFF SSGQVCTNGT RVFIHRSQQA
310 320 330 340 350
RFEAKVLERV QRIRLGDPQD ENTNFGPLVS FPHMESVLGY IESGKAQKAR
360 370 380 390 400
LLCGGERVTD GAFGKGAYVA PTVFTDCRDD MTIVREEIFG PVMSILVYDD
410 420 430 440 450
EDEAIRRAND TEYGLAAGVV TQDLARAHRA IHRLEAGICW INTWGESPAE
460 470 480 490
MPVGGYKQSG VGRENGLTTL AHYTRIKSVQ VELGDYASVF
Length:490
Mass (Da):53,332
Last modified:March 1, 2001 - v1
Checksum:iF48249A085E3A970
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG08758.1.
PIRiF82973.
RefSeqiNP_254060.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG08758; AAG08758; PA5373.
GeneIDi881619.
KEGGipae:PA5373.
PATRICi19845617. VBIPseAer58763_5630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG08758.1 .
PIRi F82973.
RefSeqi NP_254060.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WME X-ray 2.10 A/B/C/D/E/F/G/H 1-490 [» ]
2WOX X-ray 2.30 A/B/C/D 2-490 [» ]
2XDR X-ray 2.30 A/B/C/D 2-490 [» ]
3ZQA X-ray 2.45 A/B/C/D 1-490 [» ]
ProteinModelPortali Q9HTJ1.
SMRi Q9HTJ1. Positions 2-490.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA5373.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG08758 ; AAG08758 ; PA5373 .
GeneIDi 881619.
KEGGi pae:PA5373.
PATRICi 19845617. VBIPseAer58763_5630.

Organism-specific databases

PseudoCAPi PA5373.

Phylogenomic databases

eggNOGi COG1012.
HOGENOMi HOG000271505.
InParanoidi Q9HTJ1.
KOi K00130.
OMAi CTDEMTI.
OrthoDBi EOG6BS8QW.
PhylomeDBi Q9HTJ1.

Enzyme and pathway databases

UniPathwayi UPA00529 ; UER00386 .
BRENDAi 1.2.1.8. 5087.

Miscellaneous databases

EvolutionaryTracei Q9HTJ1.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. "The crystal structure of a ternary complex of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa Provides new insight into the reaction mechanism and shows a novel binding mode of the 2'-phosphate of NADP+ and a novel cation binding site."
    Gonzalez-Segura L., Rudino-Pinera E., Munoz-Clares R.A., Horjales E.
    J. Mol. Biol. 385:542-557(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH NADP AND POTASSIUM IONS, ACTIVE SITE, OXIDATION AT CYS-286, REACTION MECHANISM, COFACTOR, SUBUNIT.
  3. "A novel cysteine-NADPH covalent adduct in Pseudomonas aeruginosa betaine aldehyde dehydrogenase suggests important roles for the reduced nucleotide in the reaction mechanism."
    Diaz-Sanchez A.G., Gonzalez-Segura L., Rudino-Pinera E., Lira-Rocha A., Munoz-Clares R.A.
    Submitted (MAY-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-490 IN COMPLEX WITH NADP AND POTASSIUM IONS, SUBUNIT.
  4. "Novel NADPH-cysteine covalent adduct found in the active site of an aldehyde dehydrogenase."
    Diaz-Sanchez A.G., Gonzalez-Segura L., Rudino-Pinera E., Lira-Rocha A., Torres-Larios A., Munoz-Clares R.A.
    Biochem. J. 439:443-452(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-490 OF WILD-TYPE AND MUTANT ALA-286 IN COMPLEX WITH WITH NADP AND POTASSIUM IONS, FUNCTION, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiBETB_PSEAE
AccessioniPrimary (citable) accession number: Q9HTJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 95 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

3D-structure, Complete proteome, Reference proteome

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