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Quinone-dependent D-lactate dehydrogenase (EC 1.1.5.12) (D-lactate dehydrogenase) (D-LDH)

 DLD_CORGL               Reviewed;         571 AA.
Q8NRY8; Q6M6P4;
27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
20-JUN-2018, entry version 119.
RecName: Full=Quinone-dependent D-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000303|PubMed:21159175};
EC=1.1.5.12 {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:21159175};
AltName: Full=D-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000303|PubMed:21159175};
Short=D-LDH {ECO:0000255|HAMAP-Rule:MF_02092};
Name=dld {ECO:0000255|HAMAP-Rule:MF_02092,
ECO:0000303|PubMed:21159175};
OrderedLocusNames=Cgl0901 {ECO:0000312|EMBL:BAB98294.1};
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 /
LMG 3730 / NCIMB 10025).
Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
Corynebacterium.
NCBI_TaxID=196627;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
Ikeda M., Nakagawa S.;
"The Corynebacterium glutamicum genome: features and impacts on
biotechnological processes.";
Appl. Microbiol. Biotechnol. 62:99-109(2003).
[2]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
PubMed=21159175; DOI=10.1186/1471-2180-10-321;
Kato O., Youn J.W., Stansen K.C., Matsui D., Oikawa T., Wendisch V.F.;
"Quinone-dependent D-lactate dehydrogenase Dld (Cg1027) is essential
for growth of Corynebacterium glutamicum on D-lactate.";
BMC Microbiol. 10:321-321(2010).
-!- FUNCTION: Catalyzes the oxidation of D-lactate to pyruvate. Has
also weak activity with L-lactate and DL-2-hydroxybutyrate.
Electrons derived from D-lactate oxidation enter the electron
transport chain. Essential for growth with D-lactate as sole
carbon and energy source. {ECO:0000269|PubMed:21159175}.
-!- CATALYTIC ACTIVITY: (R)-lactate + a quinone = pyruvate + a quinol.
{ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:21159175}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000255|HAMAP-Rule:MF_02092,
ECO:0000269|PubMed:21159175};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.62 mM for D-lactate {ECO:0000269|PubMed:21159175};
Vmax=73.5 umol/min/mg enzyme {ECO:0000269|PubMed:21159175};
pH dependence:
Optimum pH is 7.0. {ECO:0000269|PubMed:21159175};
Temperature dependence:
Optimum temperature is 45 degrees Celsius.
{ECO:0000269|PubMed:21159175};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
Rule:MF_02092}; Peripheral membrane protein {ECO:0000255|HAMAP-
Rule:MF_02092}; Cytoplasmic side {ECO:0000255|HAMAP-
Rule:MF_02092}.
-!- INDUCTION: Constitutively expressed.
{ECO:0000269|PubMed:21159175}.
-!- DISRUPTION PHENOTYPE: Inactivation results in the loss of the
ability to grow with D-lactate. {ECO:0000269|PubMed:21159175}.
-!- SIMILARITY: Belongs to the quinone-dependent D-lactate
dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_02092,
ECO:0000305}.
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EMBL; BA000036; BAB98294.1; -; Genomic_DNA.
RefSeq; NP_600129.1; NC_003450.3.
RefSeq; WP_011013960.1; NC_006958.1.
ProteinModelPortal; Q8NRY8; -.
SMR; Q8NRY8; -.
STRING; 196627.cg1027; -.
EnsemblBacteria; BAB98294; BAB98294; BAB98294.
GeneID; 1018894; -.
KEGG; cgl:NCgl0865; -.
PATRIC; fig|196627.13.peg.886; -.
eggNOG; ENOG4105CXG; Bacteria.
eggNOG; COG0277; LUCA.
HOGENOM; HOG000122232; -.
KO; K03777; -.
OMA; RDRYEHH; -.
BioCyc; CORYNE:G18NG-10471-MONOMER; -.
BRENDA; 1.1.5.10; 960.
Proteomes; UP000000582; Chromosome.
GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0016901; F:oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor; IEA:InterPro.
GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
GO; GO:0019516; P:lactate oxidation; IEA:InterPro.
GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
Gene3D; 3.30.1370.20; -; 1.
Gene3D; 3.30.43.10; -; 1.
Gene3D; 3.30.70.610; -; 2.
HAMAP; MF_02092; DLDH_Dld; 1.
InterPro; IPR016172; D-lactate_DH_C-sub1.
InterPro; IPR016173; D-lactate_DH_C-sub2.
InterPro; IPR012256; D_lactate_DH.
InterPro; IPR016166; FAD-bd_2.
InterPro; IPR036318; FAD-bd_2-like_sf.
InterPro; IPR016167; FAD-bd_2_sub1.
InterPro; IPR016164; FAD-linked_Oxase-like_C.
InterPro; IPR015409; Lactate_DH_C.
InterPro; IPR006094; Oxid_FAD_bind_N.
Pfam; PF01565; FAD_binding_4; 1.
Pfam; PF09330; Lact-deh-memb; 1.
PIRSF; PIRSF000101; D-lactate_dh; 1.
SUPFAM; SSF55103; SSF55103; 1.
SUPFAM; SSF56176; SSF56176; 1.
PROSITE; PS51387; FAD_PCMH; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; FAD; Flavoprotein; Membrane;
Oxidoreductase; Quinone; Reference proteome.
CHAIN 1 571 Quinone-dependent D-lactate
dehydrogenase.
/FTId=PRO_0000441706.
DOMAIN 44 273 FAD-binding PCMH-type.
{ECO:0000255|HAMAP-Rule:MF_02092}.
NP_BIND 78 82 FAD. {ECO:0000255|HAMAP-Rule:MF_02092}.
NP_BIND 86 87 FAD. {ECO:0000255|HAMAP-Rule:MF_02092}.
BINDING 145 145 FAD; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_02092}.
BINDING 152 152 FAD. {ECO:0000255|HAMAP-Rule:MF_02092}.
BINDING 162 162 FAD; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_02092}.
BINDING 263 263 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000255|HAMAP-
Rule:MF_02092}.
SEQUENCE 571 AA; 63723 MW; 55DE9D87A864264F CRC64;
MTQPGQTTTT SHEAIDAFKR IVGDEHVLTS ERATMPFSKG YRFGGGPVFA VVRPGTLVEM
WRALQVSVDN NLIVIPQASN TGLTGGSGPG FQDYDRPIVI ISTHRIDEVH LINDAREAIS
LAGTPLTHLT DALAKHQREP HSVIGSTSIG ASVIGGIANN SGGSQIRKGP AFTREAIFAR
VNDDGKVELV NHLGISLGDD PEVALDRLQR GEWSPEDVTP APEDSNETEY AEHLRKIVPS
PARYNANPEY LFEASGSAGK LMVFAVRTRT FPREVHPTVF YIGTNNTHEL EEIRRLFLEA
DMPLPISGEY MGRSAFDLAE KYGKDTFVFL KFMSPALQTR MFSFKTWANG LFSKIPGIGP
TFADTVSQAM FSVLPNQLPK RMMEYRNRFE HHLLLTVSES QKAASEKMLK EFFAEPEHTG
EFFICTSDEE KSASLNRFGA ASAATRYAAL KRRHIAGLIP IDVALRRDDW NWLEVLPEEI
DDQLEVKAYY GHFFCHVMHQ DYVAKQGVDL EALHDRIQHL LEERGAKLPA EHNYGRIYKL
PESMEEHFKE LDPTNTFNAG IGGTSPHKDW A


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