[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=ATCC 12980 / DSM 22 / IFO 12550 / NCIB 8923 / NCTC 10339; DOI=10.1021/bi00425a026; PubMed=3069133 [NCBI, ExPASy, EBI, Israel, Japan] Nagata S., Tanizawa K., Esaki N., Sakamoto Y., Ohshima T., Tanaka H., Soda K.; "Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases."; Biochemistry 27:9056-9062(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Katoh R., Seki M., Nagata S., Misono H.; "Nucleotide sequence, cloning, overexpression and site-directed mutagenesis of the leucine dehydrogenase gene from Bacillus sphaericus."; Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[3]	ACTIVE SITE LYS-80. PubMed=1400267 [NCBI, ExPASy, EBI, Israel, Japan] Matsuyama T., Soda K., Fukui T., Tanizawa K.; "Leucine dehydrogenase from Bacillus stearothermophilus: identification of active-site lysine by modification with pyridoxal phosphate."; J. Biochem. 112:258-265(1992).

Comments

FUNCTION: Functions catabolically in the bacterial metabolism of branched-chain L-amino acids, and plays an important role in spore germination in cooperation with alanine dehydrogenase.
CATALYTIC ACTIVITY: L-leucine + H₂O + NAD⁺ = 4-methyl-2-oxopentanoate + NH₃ + NADH.
PATHWAY: Amino-acid degradation; L-leucine degradation; 4-methyl-2-oxopentanoic acid from L-leucine (dehydrogenase route): step 1/1 .
SUBUNIT: Homohexamer.
SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
SEQUENCE CAUTION:
- Sequence=AAA22570.1; Type=Frameshift; Positions=365;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M22977; AAA22570.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB103384; BAC81829.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A31950; A31950.

3D structure databases

HSSP

Q59771; 1C1D. [HSSP ENTRY / PDB]

SMR

P13154; 1-364.

ModBase

P13154.

Ontologies

GO:0050049;	Molecular function: leucine dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR006095; Glu/Leu/Phe/Val_DHase.
IPR006096; Glu/Leu/Phe/Val_DHase_C.
IPR006097; Glu/Leu/Phe/Val_DHase_dimer.
IPR016211; Glu/Phe/Leu/Val_DHase_bac/arc.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00208; ELFV_dehydrog; 1.
PF02812; ELFV_dehydrog_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000188; Phe_leu_dh; 1.

PRINTS

PR00082; GLFDHDRGNASE.

PROSITE

PS00074; GLFV_DEHYDROGENASE; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Branched-chain amino acid catabolism; Direct protein sequencing; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 367`	`367`	`Leucine dehydrogenase.`	`PRO_0000182803`
`NP_BIND`	`180 186`	`7`	`NAD (Potential).`
`ACT_SITE`	`80 80`
`CONFLICT`	`350 352`		`RSP -> ASQ (in Ref. 1; AAA22570).`

Sequence information

Length: 367 AA [This is the length of the unprocessed precursor]

Molecular weight: 40458 Da [This is the MW of the unprocessed precursor]

CRC64: E01E7086453D33DD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MELFKYMETY DYEQVLFCQD KESGLKAIIA IHDTTLGPAL GGTRMWMYNS EEEALEDALR 

        70         80         90        100        110        120 
LARGMTYKNA AAGLNLGGGK TVIIGDPRKD KNEAMFRAFG RFIQGLNGRY ITAEDVGTTV 

       130        140        150        160        170        180 
ADMDIIYQET DYVTGISPEF GSSGNPSPAT AYGVYRGMKA AAKEAFGSDS LEGKVVAVQG 

       190        200        210        220        230        240 
VGNVAYHLCR HLHEEGAKLI VTDINKEVVA RAVEEFGAKA VDPNDIYGVE CDIFAPCALG 

       250        260        270        280        290        300 
GIINDQTIPQ LKAKVIAGSA DNQLKEPRHG DIIHEMGIVY APDYVINAGG VINVADELYG 

       310        320        330        340        350        360 
YNRERAMKKI EQIYDNIEKV FAIAKRDNIP TYVAADRMAE ERIETMRKAR SPFLQNGHHI 


LSRRRAR

P13154 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools