[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Gaspar P., Coelho P., Neves A.R., Shearman C.A., Gasson M.J., Soares C.M., Baptisa A.M., Ramos A., Santos H.; "Characterization of a lactate dehydrogenase encoded by the ldhB gene of Lactococcus lactis."; Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: (S)-lactate + NAD⁺ = pyruvate + NADH.
PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1 .
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the LDH/MDH superfamily. LDH 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

AY236961; AAP49572.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

P0C2T6.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004459;	Molecular function: L-lactate dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0019642;	Biological process: anaerobic glycolysis (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00488; -; 1.
PBIL [Tree]

InterPro

IPR001557; L-lactate/malate_DHase.
IPR011304; L-lactate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.110.10; lact_mal_DH; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000102; Lac_mal_DH; 1.

PRINTS

PR00086; LLDHDRGNASE.

TIGRFAMs

TIGR01771; L-LDH-NAD; 1.

PS00064; L_LDH; 1.

Other

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

Keywords

Cytoplasm; Glycolysis; NAD; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 314`	`314`	`L-lactate dehydrogenase 2.`	`PRO_0000168355`
`NP_BIND`	`14 42`	`29`	`NAD (By similarity).`
`ACT_SITE`	`178 178`		`Proton acceptor (By similarity).`
`BINDING`	`91 91`		`Substrate (By similarity).`
`BINDING`	`123 123`		`NAD or substrate (By similarity).`
`BINDING`	`154 154`		`Substrate (By similarity).`
`BINDING`	`232 232`		`Substrate (By similarity).`
`MOD_RES`	`223 223`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 314 AA [This is the length of the unprocessed precursor]

Molecular weight: 34398 Da [This is the MW of the unprocessed precursor]

CRC64: 9D5114712ACB75A4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKITSRKVVV IGTGFVGTSI AYSMINQGLV NELVLIDVNQ DKAEGEALDL LDGISWAQEN 

        70         80         90        100        110        120 
VIVRAGNYKD CENADIVVIT AGVNQKPGQS RLDLVNTNAK IMRSIVTQVM DSGFDGIFVI 

       130        140        150        160        170        180 
ASNPVDILTY VAWETSGLDQ SRIVGTGTTL DTTRFRKELA TKLEIDPRSV HGYIIGEHGD 

       190        200        210        220        230        240 
SEVAVWSHTT IGGKPILEFI VKNKKIGLED LSNLSNKVKN AAYEIIDKKQ ATYYGIGMST 

       250        260        270        280        290        300 
ARIVKAILNN EQVILPVSAY LRGEYGQEGV FTGVPSVVNQ NGVREIIELN IDAYEMKQFE 

       310 
KSVSQLKEVI ESIK

P0C2T6 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