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P0A393

- DHLE_BACCE

UniProt

P0A393 - DHLE_BACCE

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Protein
Leucine dehydrogenase
Gene
ldh
Organism
Bacillus cereus
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei82 – 821 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi182 – 1887NAD Reviewed prediction

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 dehydrogenase
PRO_0000182800Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP0A393.
SMRiP0A393. Positions 3-366.

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

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MTLEIFEYLE KYDYEQVVFC QDKESGLKAI IAIHDTTLGP ALGGTRMWTY    50
DSEEAAIEDA LRLAKGMTYK NAAAGLNLGG AKTVIIGDPR KDKSEAMFRA 100
LGRYIQGLNG RYITAEDVGT TVDDMDIIHE ETDFVTGISP SFGSSGNPSP 150
VTAYGVYRGM KAAAKEAFGT DNLEGKVIAV QGVGNVAYHL CKHLHAEGAK 200
LIVTDINKEA VQRAVEEFGA SAVEPNEIYG VECDIYAPCA LGATVNDETI 250
PQLKAKVIAG SANNQLKEDR HGDIIHEMGI VYAPDYVINA GGVINVADEL 300
YGYNRERALK RVESIYDTIA KVIEISKRDG IATYVAADRL AEERIASLKN 350
SRSTYLRNGH DIISRR 366
Length:366
Mass (Da):39,867
Last modified:March 15, 2005 - v1
Checksum:iDA84E58062E772AC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U51099 Genomic DNA. Translation: AAA96314.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U51099 Genomic DNA. Translation: AAA96314.1 .

3D structure databases

ProteinModelPortali P0A393.
SMRi P0A393. Positions 3-366.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00363 ; UER00858 .

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR006095. 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 ]
PANTHERi PTHR11606:SF3. PTHR11606:SF3. 1 hit.
Pfami PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000188. Phe_leu_dh. 1 hit.
PRINTSi PR00082. GLFDHDRGNASE.
SMARTi SM00839. ELFV_dehydrog. 1 hit.
[Graphical view ]
PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 43 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

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