RegulonDB RegulonDB 11.1: Gene Form
   

dld gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

bglX dld pbpG TSS_2451 TSS_2451 TSS_2450 TSS_2450 dldp6 dldp6 bglXp bglXp dldp7 dldp7 TSS_2448 TSS_2448 TSS_2447 TSS_2447 TSS_2446 (cluster) TSS_2446 (cluster) TSS_2445 TSS_2445

Gene      
Name: dld    Texpresso search in the literature
Synonym(s): ECK2126, EG10231, b2133, ldh
Genome position(nucleotides): 2222185 --> 2223900
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 52.21
External database links:  
ASAP:
 ABE-0007048
CGSC:
 852
ECHOBASE:
 EB0227
ECOLIHUB:
 dld
OU-MICROARRAY:
 b2133
STRING:
 511145.b2133
COLOMBOS: dld


Product      
Name: quinone-dependent D-lactate dehydrogenase
Synonym(s): Dld, Ldh
Sequence: Get amino acid sequence Fasta Format
Cellular location: inner membrane
Molecular weight: 64.612
Isoelectric point: 6.649
Motif(s):
 
Type Positions Sequence Comment
1 -> 268 MSSMTTTDNKAFLNELARLVGSSHLLTDPAKTARYRKGFRSGQGDALAVVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPNGNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGPAYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDDDRIKDDDVRHDGRHAHDYDYVHRVRDIEADTPARYNADPDRLFESSGCAGKLAVFAVRLD FAD binding domain
2 -> 571 SSMTTTDNKAFLNELARLVGSSHLLTDPAKTARYRKGFRSGQGDALAVVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPNGNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGPAYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDDDRIKDDDVRHDGRHAHDYDYVHRVRDIEADTPARYNADPDRLFESSGCAGKLAVFAVRLDTFEAEKNQQVFYIGTNQPEVLTEIRRHILANFENLPVAGEYMHRDIYDIAEKYGKDTFLMIDKLGTDKMPFFFNLKGRTDAMLEKVKFFRPHFTDRAMQKFGHLFPSHLPPRMKNWRDKYEHHLLLKMAGDGVGEAKSWLVDYFKQAEGDFFVCTPEEGSKAFLHRFAAAGAAIRYQAVHSDEVEDILALDIALRRNDTEWYEHLPPEIDSQLVHKLYYGHFMCYVFHQDYIVKKGVDVHALKEQMLELLQQRGAQYPAEHNVGHLYKAPETLQKFYRENDPTNSMNPGIGKTSKRKNWQEVE UniProt: Quinone-dependent D-lactate dehydrogenase.
42 -> 213 GQGDALAVVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPNGNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGPAYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDDDRIKD UniProt: FAD-binding PCMH-type.
47 -> 166 LAVVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPNGNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQR
76 -> 80 AANTG UniProt: FAD.

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.3 - energy metabolism, carbon --> 1.3.6 - aerobic respiration
  1 - metabolism --> 1.4 - energy production/transport --> 1.4.1 - electron donors
  6 - cell structure --> 6.1 - membrane
Gene Ontology Terms (GO)  
cellular_component GO:0016020 - membrane
GO:0005886 - plasma membrane
GO:0005887 - integral component of plasma membrane
GO:0031234 - extrinsic component of cytoplasmic side of plasma membrane
molecular_function GO:0102029 - D-lactate dehydrogenase (quinone) activity
GO:0003824 - catalytic activity
GO:0009055 - electron transfer activity
GO:0016491 - oxidoreductase activity
GO:0016901 - oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor
GO:0050660 - flavin adenine dinucleotide binding
GO:0048038 - quinone binding
GO:0071949 - FAD binding
biological_process GO:0009060 - aerobic respiration
GO:0009061 - anaerobic respiration
GO:0006089 - lactate metabolic process
GO:0022904 - respiratory electron transport chain
GO:0055085 - transmembrane transport
GO:0019516 - lactate oxidation
Note(s): Note(s): ...[more].
Reference(s): [1] Barnes EM., et al., 1971
[2] Barnes EM., et al., 1970
[3] Campbell HD., et al., 1984
[4] George-Nascimento C., et al., 1976
[5] Ho C., et al., 1989
[6] Ingledew WJ., et al., 1984
[7] Kaback HR., et al., 1970
[8] Lawford HG., et al., 1973
[9] Reeves JP. 1971
[10] Reeves JP., et al., 1973
[11] Rule GS., et al., 1985
[12] Rule GS., et al., 1987
[13] Santos E., et al., 1982
[14] Short SA., et al., 1975
[15] Short SA., et al., 1975
[16] Short SA., et al., 1974
[17] Tanaka Y., et al., 1976
[18] Truong HT., et al., 1991
[19] Truong HT., et al., 1991
[20] Young IG., et al., 1982
External database links:  
ALPHAFOLD:
 P06149
ECOCYC:
 DLACTDEHYDROGFAD-MONOMER
ECOLIWIKI:
 b2133
INTERPRO:
 IPR016173
INTERPRO:
 IPR036318
INTERPRO:
 IPR016172
INTERPRO:
 IPR016169
INTERPRO:
 IPR016167
INTERPRO:
 IPR016166
INTERPRO:
 IPR016164
INTERPRO:
 IPR015409
INTERPRO:
 IPR012256
INTERPRO:
 IPR006094
MODBASE:
 P06149
PDB:
 1F0X
PFAM:
 PF01565
PFAM:
 PF09330
PRIDE:
 P06149
PROSITE:
 PS51387
REFSEQ:
 NP_416637
SMR:
 P06149
UNIPROT:
 P06149


Operon      
Name: dld         
Operon arrangement:
Transcription unit        Promoter
dld


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_2445 2220276 reverse nd [RS-EPT-CBR] [21]
  promoter TSS_2446 (cluster) 2220896 reverse nd [RS-EPT-CBR] [21]
  promoter TSS_2447 2220929 reverse nd [RS-EPT-CBR] [21]
  promoter TSS_2448 2222042 reverse nd [RS-EPT-CBR] [21]
  promoter dldp7 2222082 forward nd [COMP-AINF] [22]
  promoter dldp6 2222152 forward nd [COMP-AINF], [RS-EPT-CBR] [21], [22]
  promoter TSS_2450 2222154 forward nd [RS-EPT-CBR] [21]
  promoter TSS_2451 2223795 forward nd [RS-EPT-CBR] [21]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

 [COMP-AINF] Inferred computationally without human oversight


Reference(s)    

 [1] Barnes EM., Kaback HR., 1971, Mechanisms of active transport in isolated membrane vesicles. I. The site of energy coupling between D-lactic dehydrogenase and beta-galactoside transport in Escherichia coli membrane vesicles., J Biol Chem 246(17):5518-22

 [2] Barnes EM., Kaback HR., 1970, Beta-galactoside transport in bacterial membrane preparations: energy coupling via membrane-bounded D-lactic dehydrogenase., Proc Natl Acad Sci U S A 66(4):1190-8

 [3] Campbell HD., Rogers BL., Young IG., 1984, Nucleotide sequence of the respiratory D-lactate dehydrogenase gene of Escherichia coli., Eur J Biochem 144(2):367-73

 [4] George-Nascimento C., Wakil SJ., Short SA., Kaback HR., 1976, Effect of lipids on the reconstitution of D-lactate oxidase in Escherichia coli membrane vesicles., J Biol Chem 251(21):6662-6

 [5] Ho C., Pratt EA., Rule GS., 1989, Membrane-bound D-lactate dehydrogenase of Escherichia coli: a model for protein interactions in membranes., Biochim Biophys Acta 988(2):173-84

 [6] Ingledew WJ., Poole RK., 1984, The respiratory chains of Escherichia coli., Microbiol Rev 48(3):222-71

 [7] Kaback HR., Milner LS., 1970, Relationship of a membrane-bound D-(-)-lactic dehydrogenase to amino acid transport in isolated bacterial membrane preparations., Proc Natl Acad Sci U S A 66(3):1008-15

 [8] Lawford HG., Haddock BA., 1973, Respiration-driven proton translocation in Escherichia coli., Biochem J 136(1):217-20

 [9] Reeves JP., 1971, Transient pH changes during D-lactate oxidation by membrane vesicles., Biochem Biophys Res Commun 45(4):931-6

 [10] Reeves JP., Hong JS., Kaback HR., 1973, Reconstitution of D-lactate-dependent transport in membrane vesicles from a D-lactate dehydrogenase mutant of Escherichia coli., Proc Natl Acad Sci U S A 70(7):1917-21

 [11] Rule GS., Pratt EA., Chin CC., Wold F., Ho C., 1985, Overproduction and nucleotide sequence of the respiratory D-lactate dehydrogenase of Escherichia coli., J Bacteriol 161(3):1059-68

 [12] Rule GS., Pratt EA., Simplaceanu V., Ho C., 1987, Nuclear magnetic resonance and molecular genetic studies of the membrane-bound D-lactate dehydrogenase of Escherichia coli., Biochemistry 26(2):549-56

 [13] Santos E., Kung H., Young IG., Kaback HR., 1982, In vitro synthesis of the membrane-bound D-lactate dehydrogenase of Escherichia coli., Biochemistry 21(9):2085-91

 [14] Short SA., Kaback HR., Hawkins T., Kohn LD., 1975, Immunochemical properties of the membrane-bound D-lactate dehydrogenase from Escherichia coli., J Biol Chem 250(11):4285-90

 [15] Short SA., Kaback HR., Kohn LD., 1975, Localization of D-lactate dehydrogenase in native and reconstituted Escherichia coli membrane vesicles., J Biol Chem 250(11):4291-6

 [16] Short SA., Kaback HR., Kohn LD., 1974, D-lactate dehydrogenase binding in Escherichia coli dld- membrane vesicles reconstituted for active transport., Proc Natl Acad Sci U S A 71(4):1461-5

 [17] Tanaka Y., Anraku Y., Futai M., 1976, Escherichia coli membrane D-lactate dehydrogenase. Isolation of the enzyme in aggregated from and its activation by Triton X-100 and phospholipids., J Biochem 80(4):821-30

 [18] Truong HT., Pratt EA., Ho C., 1991, Interaction of the membrane-bound D-lactate dehydrogenase of Escherichia coli with phospholipid vesicles and reconstitution of activity using a spin-labeled fatty acid as an electron acceptor: a magnetic resonance and biochemical study., Biochemistry 30(16):3893-8

 [19] Truong HT., Pratt EA., Rule GS., Hsue PY., Ho C., 1991, Inactive and temperature-sensitive folding mutants generated by tryptophan substitutions in the membrane-bound d-lactate dehydrogenase of Escherichia coli., Biochemistry 30(44):10722-9

 [20] Young IG., Jaworowski A., Poulis M., 1982, Cloning of the gene for the respiratory D-lactate dehydrogenase of Escherichia coli., Biochemistry 21(9):2092-5

 [21] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

 [22] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78

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