Reviewed, UniProtKB/Swiss-Prot Q6HBQ8 (LDH3_BACHK)

Names and origin

Protein names

Recommended name:
    L-lactate dehydrogenase 3
      Short name=L-LDH 3
    EC=1.1.1.27

Gene names

Name:	ldh3
Ordered Locus Names:	BT9727_4708

Organism

Bacillus thuringiensis subsp. konkukian [Complete proteome] [HAMAP]

Taxonomic identifier

180856 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	(S)-lactate + NAD+ = pyruvate + NADH. HAMAP MF_00488
Pathway	Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. HAMAP MF_00488
Subunit structure	Homotetramer By similarity. HAMAP MF_00488
Subcellular location	Cytoplasm By similarity HAMAP MF_00488.
Sequence similarities	Belongs to the LDH/MDH superfamily. LDH family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	anaerobic glycolysis Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-lactate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 316	316	L-lactate dehydrogenase 3 HAMAP MF_00488		PRO_0000237543
Regions
	Nucleotide binding	14 – 42	29	NAD By similarity
Sites
	Active site	178	1	Proton acceptor HAMAP MF_00488
	Binding site	91	1	Substrate By similarity
	Binding site	123	1	NAD or substrate By similarity
	Binding site	154	1	Substrate By similarity
	Binding site	233	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6HBQ8-1 [UniParc]. Last modified May 30, 2006. Version 2. Checksum: CE4B64686E72E1DF	FASTA	316	34,798
	10 20 30 40 50 60 MKRHTRKIAI IGTGLVGSSC AYSIVNQGIC EELLLIDINH ERAVGEAMDL SHCINFTNTR 70 80 90 100 110 120 TKVYAGSYED CKDMDIVIIT AGPAPKPGQS RLDTLGASAK IMESVVGGVM ESGFDGIFLL 130 140 150 160 170 180 ASNPVDIITY QVWKLSGLPR NRVIGTGTSL DSSRLRTILS EMLHVDPRSI HGYSLGEHGD 190 200 210 220 230 240 SQMVAWSHVT VGGKPILQIL EEQKERFGEI DLDEIVEKTA KAGWEIYKRK GTTYYGIGNS 250 260 270 280 290 300 LAYIANSIFN DDHRVIAVSA ILDGEYGEYD ICTGVPAIIT RDGIREIVEL NLTEDEESRF 310 AKSNDILRDY MKTIGY

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT63957.1. Different initiation.
RefSeq	YP_039018.1.
3D structure databases
SMR	Q6HBQ8. Positions 5-313.
ModBase	Search...
Genome annotation databases
GeneID	2853614.
GenomeReviews	Gene locus BT9727_4708 in contig AE017355_GR.
KEGG	btk:BT9727_4708.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG566126.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_4708-MONOMER.
Family and domain databases
HAMAP	MF_00488. Lactate_dehydrog. [Tree]
InterPro	IPR001557. L-lactate/malate_DH. IPR011304. L-lactate_DH. IPR018177. L-lactate_DH_AS. IPR001236. Lactate/malate_DH. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view]
PIRSF	PIRSF000102. Lac_mal_DH. 1 hit.
PRINTS	PR00086. LLDHDRGNASE.
TIGRFAMs	TIGR01771. L-LDH-NAD. 1 hit.
PROSITE	PS00064. L_LDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LDH3_BACHK

Accession

Primary (citable) accession number: Q6HBQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	May 30, 2006
Last modified:	February 9, 2010
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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