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Q92YD2 (BETB2_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NAD/NADP-dependent betaine aldehyde dehydrogenase 2

Short name=BADH 2
EC=1.2.1.8
Gene names
Name:betB2
Ordered Locus Names:RA0952
ORF Names:SMa1731
Encoded onPlasmid pSymA (megaplasmid 1)
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid By similarity. HAMAP-Rule MF_00804

Catalytic activity

Betaine aldehyde + NAD+ + H2O = betaine + NADH. HAMAP-Rule MF_00804

Cofactor

Binds 2 potassium ions per subunit By similarity. HAMAP-Rule MF_00804

Pathway

Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. HAMAP-Rule MF_00804

Subunit structure

Dimer of dimers By similarity. HAMAP-Rule MF_00804

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence caution

The sequence AAK65610.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   LigandMetal-binding
NAD
NADP
Potassium
   Molecular functionOxidoreductase
   PTMOxidation
   Technical termComplete proteome
Plasmid
Gene Ontology (GO)
   Biological_processglycine betaine biosynthetic process from choline

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionbetaine-aldehyde dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 481481NAD/NADP-dependent betaine aldehyde dehydrogenase 2 HAMAP-Rule MF_00804
PRO_0000056554

Regions

Nucleotide binding152 – 1554NAD/NADP By similarity
Nucleotide binding178 – 1814NAD/NADP By similarity
Nucleotide binding230 – 2356NAD/NADP By similarity

Sites

Active site1641Charge relay system By similarity
Active site2521Proton acceptor By similarity
Active site4601Charge relay system By similarity
Metal binding291Potassium 1 By similarity
Metal binding961Potassium 1 By similarity
Metal binding1821Potassium 1; via carbonyl oxygen By similarity
Metal binding2461Potassium 2; via carbonyl oxygen By similarity
Metal binding4531Potassium 2; via carbonyl oxygen By similarity
Metal binding4561Potassium 2; via carbonyl oxygen By similarity
Binding site2111NAD/NADP; via amide nitrogen By similarity
Binding site2861NAD/NADP By similarity
Binding site3831NAD/NADP By similarity

Amino acid modifications

Modified residue2861Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92YD2 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: 8C21F9C596E54988

FASTA48151,097
        10         20         30         40         50         60 
MATPLCQPAA SHFIDGTFIE DRTGPEILSV NPVDGEIIAK LHGATSCIIE KAIASAKRAQ 

        70         80         90        100        110        120 
KEWARKEPAE RGRVLSRAAD IMRARNRELS VLETRDTGKP ISETLVADAA SGADCLEYFG 

       130        140        150        160        170        180 
AIAATLSGDS IQFGEDWVYT RREPLGVCLG IGAWNYPIQI AAWKAAPALA CGNAMIFKPS 

       190        200        210        220        230        240 
EVTPLSALKL AEILTEAGLP PGVFNIVQGA GDVGAELATH PAIAKVSLTG SVKTGARVAS 

       250        260        270        280        290        300 
AAMAGIRPVT MELGGKSALI VFDDADVEAA VSGAILGNFY SAGQICSNGT RVFLQRGIRE 

       310        320        330        340        350        360 
AFLARLLARV AALKIGDPMD EETDIGPLVS AAHRNRVATY VARAEVEGAY QMAPPRKLPP 

       370        380        390        400        410        420 
GDAWHEPVVF TNVTDWMTLA REEVFGPVMA VLDFDDEQDV VARANATDFG LAAGIFTRDL 

       430        440        450        460        470        480 
VRAHRLAAEL EAGTVWINAY NLTPAGMAFG GIKRSGIGRE NGRVAIDHYT QLKSVFVSMQ 


T 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006469 Genomic DNA. Translation: AAK65610.1. Different initiation.
PIRH95380.
RefSeqNP_436198.1. NC_003037.1.

3D structure databases

ProteinModelPortalQ92YD2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SMa1731.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK65610; AAK65610; SMa1731.
GeneID1235988.
KEGGsme:SMa1731.
PATRIC23628404. VBISinMel96828_0981.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
KOK00130.
OrthoDBEOG6BS8QW.
ProtClustDBPRK13252.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-5958-MONOMER.
UniPathwayUPA00529; UER00386.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPMF_00804. BADH.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR011264. BADH.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBETB2_RHIME
AccessionPrimary (citable) accession number: Q92YD2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways