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Protein

Leucine dehydrogenase

Gene

ldh

Organism
Bacillus cereus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible deamination of L-leucine to 4-methyl-2-oxopentanoate.1 Publication

Catalytic activityi

L-leucine + H2O + NAD+ = 4-methyl-2-oxopentanoate + NH3 + NADH.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei82 – 821PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi182 – 1887NADSequence Analysis

GO - Molecular functioni

  1. leucine dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. leucine catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Branched-chain amino acid catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00363; UER00858.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine dehydrogenase (EC:1.4.1.9)
Short name:
LeuDH
Gene namesi
Name:ldh
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Leucine dehydrogenasePRO_0000182800Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP0A393.
SMRiP0A393. Positions 3-366.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016211. Glu/Phe/Leu/Val_DH_bac/arc.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11606:SF3. PTHR11606:SF3. 1 hit.
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000188. Phe_leu_dh. 1 hit.
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A393-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLEIFEYLE KYDYEQVVFC QDKESGLKAI IAIHDTTLGP ALGGTRMWTY
60 70 80 90 100
DSEEAAIEDA LRLAKGMTYK NAAAGLNLGG AKTVIIGDPR KDKSEAMFRA
110 120 130 140 150
LGRYIQGLNG RYITAEDVGT TVDDMDIIHE ETDFVTGISP SFGSSGNPSP
160 170 180 190 200
VTAYGVYRGM KAAAKEAFGT DNLEGKVIAV QGVGNVAYHL CKHLHAEGAK
210 220 230 240 250
LIVTDINKEA VQRAVEEFGA SAVEPNEIYG VECDIYAPCA LGATVNDETI
260 270 280 290 300
PQLKAKVIAG SANNQLKEDR HGDIIHEMGI VYAPDYVINA GGVINVADEL
310 320 330 340 350
YGYNRERALK RVESIYDTIA KVIEISKRDG IATYVAADRL AEERIASLKN
360
SRSTYLRNGH DIISRR
Length:366
Mass (Da):39,867
Last modified:March 15, 2005 - v1
Checksum:iDA84E58062E772AC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51099 Genomic DNA. Translation: AAA96314.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51099 Genomic DNA. Translation: AAA96314.1.

3D structure databases

ProteinModelPortaliP0A393.
SMRiP0A393. Positions 3-366.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00363; UER00858.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016211. Glu/Phe/Leu/Val_DH_bac/arc.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11606:SF3. PTHR11606:SF3. 1 hit.
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000188. Phe_leu_dh. 1 hit.
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing and overexpression of the leucine dehydrogenase gene from Bacillus cereus."
    Stoyan T., Recktenwald A., Kula M.R.
    J. Biotechnol. 54:77-80(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18; 47-56; 160-192; 214-254 AND 279-298, FUNCTION, CATALYTIC ACTIVITY.
    Strain: DSM 626.

Entry informationi

Entry nameiDHLE_BACCE
AccessioniPrimary (citable) accession number: P0A393
Secondary accession number(s): Q59194
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: October 1, 2014
This is version 44 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

Direct protein sequencing

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.