[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1016/S0140-6736(00)04403-2; PubMed=11418146 [NCBI, ExPASy, EBI, Israel, Japan] Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.; "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; Lancet 357:1225-1240(2001).
[2]	IDENTIFICATION BY MASS SPECTROMETRY. Stenz L.; "Shotgun proteomic analysis of total protein extract of S. aureus S30 versus N315."; Submitted (NOV-2005) to UniProtKB.
[3]	IDENTIFICATION BY MASS SPECTROMETRY. Vaezzadeh A.R., Deshusses J., Lescuye P., Hochstrasser D.F.; "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."; Submitted (OCT-2007) to UniProtKB.

Comments

FUNCTION: Appears to be the primary factor that allows S.aureus growth during nitrosative stress in both aerobically and anaerobically cultured cells (By similarity).
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

BA000018; BAB41455.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D89787; D89787.

RefSeq

NP_373477.1; -.

3D structure databases

HSSP

P00344; 2LDB. [HSSP ENTRY / PDB]

ModBase

P65256.

Enzyme and pathway databases

BioCyc

SAUR158879:SA0232-MON; -.

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).
GO:0006950;	Biological process: response to stress (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.

Genome annotation databases

GeneID

1123010; -.

GenomeReviews

BA000018_GR; SA0232.

KEGG

sau:SA0232; -.

Phylogenomic databases

HOGENOM

P65256; -.

Genome annotation databases

CMR

P65256; SA0232.

Other

UniRef

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

Keywords

Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase; Phosphoprotein; Stress response.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 317`	`317`	`L-lactate dehydrogenase 1.`	`PRO_0000168382`
`NP_BIND`	`15 43`	`29`	`NAD (By similarity).`
`ACT_SITE`	`179 179`		`Proton acceptor (By similarity).`
`BINDING`	`92 92`		`Substrate (By similarity).`
`BINDING`	`124 124`		`NAD or substrate (By similarity).`
`BINDING`	`155 155`		`Substrate (By similarity).`
`BINDING`	`232 232`		`Substrate (By similarity).`
`MOD_RES`	`223 223`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 317 AA [This is the length of the unprocessed precursor]

Molecular weight: 34569 Da [This is the MW of the unprocessed precursor]

CRC64: CDDE4813AF6CB226 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNKFKGNKVV LIGNGAVGSS YAFSLVNQSI VDELVIIDLD TEKVRGDVMD LKHATPYSPT 

        70         80         90        100        110        120 
TVRVKAGEYS DCHDADLVVI CAGAAQKPGE TRLDLVSKNL KIFKSIVGEV MASKFDGIFL 

       130        140        150        160        170        180 
VATNPVDILA YATWKFSGLP KERVIGSGTI LDSARFRLLL SEAFDVAPRS VDAQIIGEHG 

       190        200        210        220        230        240 
DTELPVWSHA NIAGQPLKTL LEQRPEGKAQ IEQIFVQTRD AAYDIIQAKG ATYYGVAMGL 

       250        260        270        280        290        300 
ARITEAIFRN EDAVLTVSAL LEGEYDEEDV YIGVPAVINR NGIRNVVEIP LNDEEQSKFA 

       310 
HSAKTLKDIM AEAEELK

P65256 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