Reviewed, UniProtKB/Swiss-Prot Q6HC14 (LDH2_BACHK)

Names and origin

Protein names

Recommended name:
    L-lactate dehydrogenase 2
      Short name=L-LDH 2
    EC=1.1.1.27

Gene names

Name:	ldh2
Ordered Locus Names:	BT9727_4600

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.
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
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 2 HAMAP MF_00488		PRO_0000237542
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)
	Q6HC14-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 82075E6DCDDC1A76	FASTA	314	34,620
	10 20 30 40 50 60 MKKGINRVVL VGTGAVGCSY AYSMINQGVA EEFVLVDVNE AKAEGEAMDL SHAVPFSPSP 70 80 90 100 110 120 TKVWSGSYAD CKDADLVVIT AGLPQKPGET RLDLVEKNTK IFKQIVRGIM DSGFDGIFLI 130 140 150 160 170 180 ATNPVDILTY VTWKESGLPK ERVIGSGTTL DSARFRYMLG DYLDVDPRNV HAYIVGEHGD 190 200 210 220 230 240 TELPVWSHAT IGVQKLETIL ANNEQYKQED LDKIFENVRD AAYHIIERKG ATYYGIGMSL 250 260 270 280 290 300 LRVTKAILNN ENSVLTVSAY LEGQYGEKDA YVGVPAVINR EGVREIVELE LNEEEKAKFA 310 HSVKVLKETM 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
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT59099.1.
RefSeq	YP_038912.1.
3D structure databases
SMR	Q6HC14. Positions 4-311.
ModBase	Search...
Genome annotation databases
GeneID	2855808.
GenomeReviews	Gene locus BT9727_4600 in contig AE017355_GR.
KEGG	btk:BT9727_4600.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG566126.
OMA	CAGANQK.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_4600-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

LDH2_BACHK

Accession

Primary (citable) accession number: Q6HC14

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 49 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)