Reviewed, UniProtKB/Swiss-Prot P13154 (DHLE_BACST)

Names and origin

Protein names

Recommended name:
    Leucine dehydrogenase
      Short name=LeuDH
    EC=1.4.1.9

Gene names

Name:	ldh
Synonyms:	leuDH

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (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-oxopentanoate from L-leucine (dehydrogenase route): step 1/1.
Subunit structure	Homohexamer.
Sequence similarities	Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
Sequence caution	The sequence AAA22570.1 differs from that shown. Reason: Frameshift at position 365.

Ontologies

Keywords
Biological process	Branched-chain amino acid catabolism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	branched chain family amino acid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro leucine dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 367	367	Leucine dehydrogenase		PRO_0000182803
Regions
	Nucleotide binding	180 – 186	7	NAD Potential
Sites
	Active site	80	1	Ref.3
Experimental info
	Sequence conflict	350 – 352	3	RSP → ASQ in AAA22570. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P13154-1 [UniParc]. Last modified October 25, 2004. Version 3. Checksum: E01E7086453D33DD	FASTA	367	40,458
	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

References

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

Cross-references

Sequence databases
EMBL GenBank DDBJ	M22977 Genomic DNA. Translation: AAA22570.1. Frameshift. AB103384 Genomic DNA. Translation: BAC81829.1.
PIR	A31950.
3D structure databases
SMR	P13154. Positions 1-364.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.4.1.9. 266715.
Family and domain databases
InterPro	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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00208. ELFV_dehydrog. 1 hit. PF02812. ELFV_dehydrog_N. 1 hit. [Graphical view]
PIRSF	PIRSF000188. Phe_leu_dh. 1 hit.
PRINTS	PR00082. GLFDHDRGNASE.
SMART	SM00839. ELFV_dehydrog. 1 hit. [Graphical view]
PROSITE	PS00074. GLFV_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHLE_BACST

Accession

Primary (citable) accession number: P13154
Secondary accession number(s): Q76GN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	October 25, 2004
Last modified:	January 19, 2010
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)