[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. DOI=10.1016/j.mimet.2004.09.017; PubMed=15590099 [NCBI, ExPASy, EBI, Israel, Japan] Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.; "Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth."; J. Microbiol. Methods 60:247-257(2005).
[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: Contributes to S.aureus growth during nitrosative stress in both aerobically and anaerobically cultured cells, despite playing a secondary role in this resistance mechanism (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; BAB43700.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B90067; B90067.

RefSeq

NP_375721.1; -.

3D structure databases

HSSP

P00344; 2LDB. [HSSP ENTRY / PDB]

ModBase

P99119.

Enzyme and pathway databases

BioCyc

SAUR158879:SA2395-MON; -.

2D gel databases

SWISS-2DPAGE

P99119; -.

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).
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.

PROSITE

PS00064; L_LDH; 1.

BLOCKS

P99119.

Genome annotation databases

GeneID

1125324; -.

GenomeReviews

BA000018_GR; SA2395.

KEGG

sau:SA2395; -.

Phylogenomic databases

HOGENOM

P99119; -.

Genome annotation databases

CMR

P99119; SA2395.

Other

ProtoNet

P99119.

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`	`1 319`	`319`	`L-lactate dehydrogenase 2.`	`PRO_0000168389`
`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`	`231 231`		`Substrate (By similarity).`
`MOD_RES`	`222 222`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 319 AA [This is the length of the unprocessed precursor]

Molecular weight: 34432 Da [This is the MW of the unprocessed precursor]

CRC64: 7779343BCA801CED [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTFGKKVVL IGDGSVGSSY AFAMVTQGVA DEFVIIDIAK DKVKADVQDL NHGTVHSPSP 

        70         80         90        100        110        120 
VDVKAGEYED CKDADLVVIT AGAPQKPGET RLQLVEKNTK IMKSIVKSVM DSGFDGYFLI 

       130        140        150        160        170        180 
AANPVDILTR FVKEYTGLPA ERVIGSGTVL DSARLQYLIS QELGVAPSSV DASIIGEHGD 

       190        200        210        220        230        240 
TELAVWSQAN VAGISVYDTL KEQTGSEAKA EEIYVNTRDA AYEIIQAKGS TYYGIALALM 

       250        260        270        280        290        300 
RISKAILNNE NNVLNVSIQL DGQYGGHKGV YLGVPTLVNQ HGAVKIYEMP LSAEEQALFD 

       310 
KSVKILEDTF DSIKYLLED

P99119 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