ECOLI:DLD

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	dld
Protein Name(s)	D-lactate dehydrogenase Respiratory D-lactate dehydrogenase
External Links
UniProt	P06149
EMBL	M10038 X01067 U00007 U00096 AP009048
PIR	A21893
RefSeq	NP_416637.1 YP_490372.1
PDB	1F0X
PDBsum	1F0X
ProteinModelPortal	P06149
SMR	P06149
IntAct	P06149
STRING	511145.b2133
BindingDB	P06149
DrugBank	DB03147 DB00756
PaxDb	P06149
PRIDE	P06149
EnsemblBacteria	AAC75194 BAE76610
GeneID	12931458 946653
KEGG	ecj:Y75_p2095 eco:b2133
PATRIC	32119607
EchoBASE	EB0227
EcoGene	EG10231
eggNOG	COG0277
HOGENOM	HOG000122232
InParanoid	P06149
KO	K03777
OMA	RRNDRDW
OrthoDB	EOG6Z3KJX
BioCyc	EcoCyc:DLACTDEHYDROGFAD-MONOMER ECOL316407:JW2121-MONOMER MetaCyc:DLACTDEHYDROGFAD-MONOMER
EvolutionaryTrace	P06149
PRO	PR:P06149
Proteomes	UP000000318 UP000000625
Genevestigator	P06149
GO	GO:0005887 GO:0008720 GO:0050660 GO:0004457 GO:0051287 GO:0016901 GO:0008762 GO:0009060 GO:0019516 GO:0055085
Gene3D	3.30.1370.20 3.30.43.10 3.30.465.10 3.30.70.610
InterPro	IPR016169 IPR016172 IPR016173 IPR012256 IPR016166 IPR016167 IPR016164 IPR015409 IPR006094
Pfam	PF01565 PF09330
PIRSF	PIRSF000101
SUPFAM	SSF55103 SSF56176
PROSITE	PS51387

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
Contributes to	GO:0008720	D-lactate dehydrogenase activity	PMID:25650346^[1]	ECO:0000314			F	Can produced enhanced PLA synthesis	complete CACAO 10562
enables	GO:0071949	FAD binding	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000202405 SGD:S000000797 SGD:S000002337	F	Seeded From UniProt	complete
enables	GO:0051990	(R)-2-hydroxyglutarate dehydrogenase activity	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0023507 PANTHER:PTN000202405 RGD:1307976 SGD:S000002337 TAIR:locus:2115230 UniProtKB:Q8N465	F	Seeded From UniProt	complete
part_of	GO:0031234	extrinsic component of cytoplasmic side of plasma membrane	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10231 PANTHER:PTN000202405	C	Seeded From UniProt	complete
involved_in	GO:0022904	respiratory electron transport chain	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10231 PANTHER:PTN000202405	P	Seeded From UniProt	complete
involved_in	GO:0019516	lactate oxidation	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10231 PANTHER:PTN000202405	P	Seeded From UniProt	complete
enables	GO:0004458	D-lactate dehydrogenase (cytochrome) activity	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000202405 SGD:S000000797 SGD:S000002337	F	Seeded From UniProt	complete
enables	GO:0050660	flavin adenine dinucleotide binding	PMID:4582730^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0050660	flavin adenine dinucleotide binding	PMID:4575624^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0031234	extrinsic component of cytoplasmic side of plasma membrane	PMID:10944213^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0022904	respiratory electron transport chain	PMID:3013300^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019516	lactate oxidation	PMID:4582730^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019516	lactate oxidation	PMID:4575624^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016901	oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor	PMID:3013300^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009061	anaerobic respiration	PMID:4587250^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009061	anaerobic respiration	PMID:195602^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009060	aerobic respiration	PMID:3013300^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009060	aerobic respiration	PMID:195602^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009060	aerobic respiration	PMID:13628604^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0009055	electron transfer activity	PMID:7578233^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0009055	electron transfer activity	PMID:3013300^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:4582730^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:4575624^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016164	F	Seeded From UniProt	complete
part_of	GO:0005887	integral component of plasma membrane	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012256	C	Seeded From UniProt	complete
involved_in	GO:0006089	lactate metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016172 InterPro:IPR016173	P	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006094	F	Seeded From UniProt	complete
enables	GO:0016901	oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012256	F	Seeded From UniProt	complete
involved_in	GO:0019516	lactate oxidation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012256	P	Seeded From UniProt	complete
involved_in	GO:0022904	respiratory electron transport chain	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012256	P	Seeded From UniProt	complete
enables	GO:0050660	flavin adenine dinucleotide binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006094 InterPro:IPR012256 InterPro:IPR015409 InterPro:IPR016164 InterPro:IPR016172 InterPro:IPR016173 InterPro:IPR036318	F	Seeded From UniProt	complete
involved_in	GO:0055085	transmembrane transport	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR015409 InterPro:IPR016172 InterPro:IPR016173	P	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006094	P	Seeded From UniProt	complete
enables	GO:0071949	FAD binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016166	F	Seeded From UniProt	complete
enables	GO:0050660	flavin adenine dinucleotide binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000635130	F	Seeded From UniProt	complete
involved_in	GO:0019516	lactate oxidation	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000635130	P	Seeded From UniProt	complete
part_of	GO:0031234	extrinsic component of cytoplasmic side of plasma membrane	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000635130	C	Seeded From UniProt	complete
enables	GO:0016901	oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000635130	F	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F	Seeded From UniProt	complete
enables	GO:0048038	quinone binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0874	F	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-KW:KW-0997 UniProtKB-SubCell:SL-0037	C	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Zhu, Y et al. (2015) Enhancement of phenyllactic acid biosynthesis by recognition site replacement of D-lactate dehydrogenase from Lactobacillus pentosus. Biotechnol. Lett. 37 1233-41 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Kohn, LD & Kaback, HR (1973) Mechanisms of active transport in isolated bacterial membrane vesicles. XV. Purification and properties of the membrane-bound D-lactate dehydrogenase from Escherichia coli. J. Biol. Chem. 248 7012-7 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Futai, M (1973) Membrane D-lactate dehydrogenase from Escherichia coli. Purification and properties. Biochemistry 12 2468-74 PubMed GONUTS page
↑ Dym, O et al. (2000) The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme. Proc. Natl. Acad. Sci. U.S.A. 97 9413-8 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Matsushita, K & Kaback, HR (1986) D-lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase. Biochemistry 25 2321-7 PubMed GONUTS page
↑ Konings, WN & Kaback, HR (1973) Anaerobic transport in Escherichia coli membrane vesicles. Proc. Natl. Acad. Sci. U.S.A. 70 3376-81 PubMed GONUTS page
↑ ^8.0 ^8.1 Wallace, BJ & Young, IG (1977) Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Studies with a ubiA- menA- double quinone mutant. Biochim. Biophys. Acta 461 84-100 PubMed GONUTS page
↑ HAUGAARD, N (1959) D- and L-lactic acid oxidases of Escherichia coli. Biochim. Biophys. Acta 31 66-72 PubMed GONUTS page
↑ Sun, ZY et al. (1995) Stopped-flow kinetic and biophysical studies of membrane-associated D-lactate dehydrogenase of Escherichia coli. Biochim. Biophys. Acta 1252 269-77 PubMed GONUTS page

[PMID:25650346-1] Zhu, Y et al. (2015) Enhancement of phenyllactic acid biosynthesis by recognition site replacement of D-lactate dehydrogenase from Lactobacillus pentosus. Biotechnol. Lett. 37 1233-41 PubMed GONUTS page

[PMID:21873635-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:4582730-3] 3.0 ^3.1 ^3.2 Kohn, LD & Kaback, HR (1973) Mechanisms of active transport in isolated bacterial membrane vesicles. XV. Purification and properties of the membrane-bound D-lactate dehydrogenase from Escherichia coli. J. Biol. Chem. 248 7012-7 PubMed GONUTS page

[PMID:4575624-4] 4.0 ^4.1 ^4.2 Futai, M (1973) Membrane D-lactate dehydrogenase from Escherichia coli. Purification and properties. Biochemistry 12 2468-74 PubMed GONUTS page

[PMID:10944213-5] Dym, O et al. (2000) The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme. Proc. Natl. Acad. Sci. U.S.A. 97 9413-8 PubMed GONUTS page

[PMID:3013300-6] 6.0 ^6.1 ^6.2 ^6.3 Matsushita, K & Kaback, HR (1986) D-lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase. Biochemistry 25 2321-7 PubMed GONUTS page

[PMID:4587250-7] Konings, WN & Kaback, HR (1973) Anaerobic transport in Escherichia coli membrane vesicles. Proc. Natl. Acad. Sci. U.S.A. 70 3376-81 PubMed GONUTS page

[PMID:195602-8] 8.0 ^8.1 Wallace, BJ & Young, IG (1977) Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Studies with a ubiA- menA- double quinone mutant. Biochim. Biophys. Acta 461 84-100 PubMed GONUTS page

[PMID:13628604-9] HAUGAARD, N (1959) D- and L-lactic acid oxidases of Escherichia coli. Biochim. Biophys. Acta 31 66-72 PubMed GONUTS page

[PMID:7578233-10] Sun, ZY et al. (1995) Stopped-flow kinetic and biophysical studies of membrane-associated D-lactate dehydrogenase of Escherichia coli. Biochim. Biophys. Acta 1252 269-77 PubMed GONUTS page

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ECOLI:DLD

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