CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002317
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 D-lactate dehydrogenase 
Protein Synonyms/Alias
 Respiratory D-lactate dehydrogenase 
Gene Name
 dld 
Gene Synonyms/Alias
 b2133; JW2121 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
31HLLTDPAKTARYRKGacetylation[1]
112DKLHVLGKGEQVLAYacetylation[1]
129TTLYSLEKALKPLGRacetylation[1]
184ARINEDGKLTLVNHLacetylation[1]
212KLDDDRIKDDDVRHDacetylation[1]
274LDTFEAEKNQQVFYIacetylation[1]
320DIYDIAEKYGKDTFLacetylation[1]
323DIAEKYGKDTFLMIDacetylation[1]
331DTFLMIDKLGTDKMPacetylation[1]
387RMKNWRDKYEHHLLLacetylation[1]
395YEHHLLLKMAGDGVGacetylation[1]
405GDGVGEAKSWLVDYFacetylation[1]
511GVDVHALKEQMLELLacetylation[1]
536HNVGHLYKAPETLQKacetylation[1]
543KAPETLQKFYRENDPacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 
Functional Description
 First component of the membrane-bound D-lactate oxidase, which is believed to play an important role in the energization of the active transport of a variety of sugars and amino acids. 
Sequence Annotation
 DOMAIN 42 213 FAD-binding PCMH-type.  
Keyword
 3D-structure; Cell membrane; Complete proteome; Direct protein sequencing; FAD; Flavoprotein; Membrane; NAD; Oxidoreductase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 571 AA 
Protein Sequence
MSSMTTTDNK AFLNELARLV GSSHLLTDPA KTARYRKGFR SGQGDALAVV FPGSLLELWR 60
VLKACVTADK IILMQAANTG LTEGSTPNGN DYDRDVVIIS TLRLDKLHVL GKGEQVLAYP 120
GTTLYSLEKA LKPLGREPHS VIGSSCIGAS VIGGICNNSG GSLVQRGPAY TEMSLFARIN 180
EDGKLTLVNH LGIDLGETPE QILSKLDDDR IKDDDVRHDG RHAHDYDYVH RVRDIEADTP 240
ARYNADPDRL FESSGCAGKL AVFAVRLDTF EAEKNQQVFY IGTNQPEVLT EIRRHILANF 300
ENLPVAGEYM HRDIYDIAEK YGKDTFLMID KLGTDKMPFF FNLKGRTDAM LEKVKFFRPH 360
FTDRAMQKFG HLFPSHLPPR MKNWRDKYEH HLLLKMAGDG VGEAKSWLVD YFKQAEGDFF 420
VCTPEEGSKA FLHRFAAAGA AIRYQAVHSD EVEDILALDI ALRRNDTEWY EHLPPEIDSQ 480
LVHKLYYGHF MCYVFHQDYI VKKGVDVHAL KEQMLELLQQ RGAQYPAEHN VGHLYKAPET 540
LQKFYRENDP TNSMNPGIGK TSKRKNWQEV E 571 
Gene Ontology
 GO:0005887; C:integral to plasma membrane; IDA:EcoCyc.
 GO:0008720; F:D-lactate dehydrogenase activity; IEA:EC.
 GO:0009055; F:electron carrier activity; IPI:EcoCyc.
 GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
 GO:0004457; F:lactate dehydrogenase activity; IDA:EcoCyc.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0016901; F:oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor; IDA:EcoCyc.
 GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro.
 GO:0009060; P:aerobic respiration; IDA:EcoCyc.
 GO:0019516; P:lactate oxidation; IDA:EcoCyc.
 GO:0055085; P:transmembrane transport; IEA:InterPro. 
Interpro
 IPR016169; CO_DH_flavot_FAD-bd_sub2.
 IPR016172; D-lactate_DH_C-sub1.
 IPR016173; D-lactate_DH_C-sub2.
 IPR012256; D_lactate_DH.
 IPR016166; FAD-bd_2.
 IPR016167; FAD-bd_2_sub1.
 IPR016164; FAD-linked_Oxase-like_C.
 IPR015409; Lactate_DH_C.
 IPR006094; Oxid_FAD_bind_N. 
Pfam
 PF01565; FAD_binding_4
 PF09330; Lact-deh-memb 
SMART
  
PROSITE
 PS51387; FAD_PCMH 
PRINTS