Reviewed, UniProtKB/Swiss-Prot Q6HK31 (LDH1_BACHK)

Names and origin

Protein names

Recommended name:
    L-lactate dehydrogenase 1
      Short name=L-LDH 1
    EC=1.1.1.27

Gene names

Name:	ldh1
Ordered Locus Names:	BT9727_1763

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	314 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the LDH/MDH superfamily. LDH family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
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 – 314	314	L-lactate dehydrogenase 1 HAMAP MF_00488		PRO_0000237541
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	232	1	Substrate By similarity
Amino acid modifications
	Modified residue	223	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6HK31-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: A99C911C2A2306E6	FASTA	314	34,788
	10 20 30 40 50 60 MKKGINRVVL VGTGAVGCSY AYCMINQAVA EEFVLVDVNE AKAEGEAMDL SHAVPFAPAP 70 80 90 100 110 120 TRVWKGSYED CKDADLVVIT AGLPQKPGET RLDLVEKNAK IFKQIVRSIM DSGFDGIFLI 130 140 150 160 170 180 ATNPVDILTY VTWKESGLPK ERVIGSGTTL DSARFRYMLG EYFNIGPHNI HAYIIGEHGD 190 200 210 220 230 240 TELPVWSHVS VGIQKLQTLL EKDNTYNQED LDKIFINVRD AAYHIIERKG ATYYGIGMSL 250 260 270 280 290 300 LRVTKAILND ENSVLTVSAY LEGQYGQKDV YIGVPAVLNR GGVREILEVE LSEDEELKFD 310 HSVQVLKETM APVL

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
EMBLGenBankDDBJ	AE017355 Genomic DNA. Translation: AAT63370.1.
RefSeq	YP_036095.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2855355.
GenomeReviews	Gene locus BT9727_1763 in contig AE017355_GR.
KEGG	btk:BT9727_1763.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6HK31.
OMA	Q6HK31. KEEHVPQ.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_1763-MON.
Family and domain databases
HAMAP	MF_00488. [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

LDH1_BACHK

Accession

Primary (citable) accession number: Q6HK31

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	July 19, 2004
Last modified:	June 16, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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