NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-42; 69-89; 266-272 AND 309-317.
STRAIN=ATCC 33205 / DSM 43846 / IFO 14230 / JCM 3312 / T-323;
PubMed=8020469 [NCBI, ExPASy, EBI, Israel, Japan]
Ohshima T., Nishida N., Bakthavatsalam S., Kataoka K., Takada H., Yoshimura T., Esaki N., Soda K.;
"The purification, characterization, cloning and sequencing of the gene for a halostable and thermostable leucine dehydrogenase from Thermoactinomyces intermedius.";
Eur. J. Biochem. 222:305-312(1994).

Comments

FUNCTION: Functions catabolically in the bacterial metabolism of branched-chain L-amino acids. Catalyzes the reversible deamination of these branched-chain L-amino acids to their oxo analogs.
CATALYTIC ACTIVITY: L-leucine + H₂O + NAD⁺ = 4-methyl-2-oxopentanoate + NH₃ + NADH.
BIOPHYSICOCHEMICAL PROPERTIES:

Temperature dependence: Thermostable;
PATHWAY: Amino-acid degradation; L-leucine degradation; 4-methyl-2-oxopentanoic acid from L-leucine (dehydrogenase route): step 1/1 .
SUBUNIT: Homooctamer.
SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

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

X79068; CAA55671.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S45607; S45607.

3D structure databases

HSSP

Q59771; 1C1D. [HSSP ENTRY / PDB]

SMR

Q60030; 1-362.

ModBase

Q60030.

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`	`1 366`	`366`	`Leucine dehydrogenase.`	`PRO_0000182805`
`NP_BIND`	`180 186`	`7`	`NAD (Potential).`
`ACT_SITE`	`80 80`		`By similarity.`

Sequence information

Length: 366 AA [This is the length of the unprocessed precursor]

Molecular weight: 40586 Da [This is the MW of the unprocessed precursor]

CRC64: 4830BF118AD656AE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIFDYMEKY DYEQLVMCQD KESGLKAIIC IHVTTLGPAL GGMRMWTYAS EEEAIEDALR 

        70         80         90        100        110        120 
LGRGMTYKNA AAGLNLGGGK TVIIGDPRKD KNEAMFRALG RFIQGLNGRY ITAEDVGTTV 

       130        140        150        160        170        180 
EDMDIIHEET RYVTGVSPAF GSSGNPSPVT AYGVYRGMKA AAKEAFGDDS LEGKVVAVQG 

       190        200        210        220        230        240 
VGHVAYELCK HLHNEGAKLI VTDINKENAD RAVQEFGAEF VHPDKIYDVE CDIFAPCALG 

       250        260        270        280        290        300 
AIINDETIER LKCKVVAGSA NNQLKEERHG KMLEEKGIVY APDYVINAGG VINVADELLG 

       310        320        330        340        350        360 
YNRERAMKKV EGIYDKILKV FEIAKRDGIP SYLAADRMAE ERIEMMRKTR STFLQDQRNL 


INFNNK

Q60030 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