NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=TSN9;
DOI=10.1007/s002530050578; PubMed=8597545 [NCBI, ExPASy, EBI, Israel, Japan]
Nagata S., Bakthavatsalam S., Galkin A.G., Asada H., Sakai S., Esaki N., Soda K., Ohshima T., Nagasaki S., Misono H.;
"Gene cloning, purification, and characterization of thermostable and halophilic leucine dehydrogenase from a halophilic thermophile, Bacillus licheniformis TSN9.";
Appl. Microbiol. Biotechnol. 44:432-438(1995).

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 (By similarity).
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 (By similarity).
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

S81735; AAB36205.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q59771; 1C1D. [HSSP ENTRY / PDB]

SMR

Q53560; 1-364.

ModBase

Q53560.

Ontologies

GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0050049;	Molecular function: leucine dehydrogenase activity (inferred from electronic annotation from EC).
GO:0009083;	Biological process: branched chain family amino acid catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

ProtoNet

Q53560.

Other

UniRef

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

Keywords

Branched-chain amino acid catabolism; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 364`	`364`	`Leucine dehydrogenase.`	`PRO_0000182802`
`NP_BIND`	`180 186`	`7`	`NAD (Potential).`
`ACT_SITE`	`80 80`		`By similarity.`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 40040 Da [This is the MW of the unprocessed precursor]

CRC64: A13A967F6E84F873 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MELFRYMEQY DYEQLVFCQD KQSGLKAIIA IHDTTLGPAL GGTRMWTYES EEAAIEDALR 

        70         80         90        100        110        120 
LARGMTYKNA AAGLNLGGGK TVIIGDPRKD KNEEMFRAFG RYIQGLNGRY ITAEDVGTTV 

       130        140        150        160        170        180 
EDMDIIHDET DFVTGISPAF GSSGNPSPVT AYGVYKGMKA AAKAAFGTDS LEGKTVAVQG 

       190        200        210        220        230        240 
VGNVAYNLCR HLHEEGAKLI VTDINKEAVE RAVAEFGARA VDPDDIYSQE CDIYAPCALG 

       250        260        270        280        290        300 
ATINDDTIPQ LKAKVIAGAA NNQLKETRHG DQIHDMGIVY APDYVINAGG VINVADELYG 

       310        320        330        340        350        360 
YNSERALKKV EGIYGNIERV LEISKRDRIP TYLAADRLAE ERIERMRQSR SQFLQNGHHI 


LSRR

Q53560 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