DLD_CORGL
ID DLD_CORGL Reviewed; 571 AA.
AC Q8NRY8; Q6M6P4;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Quinone-dependent D-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000303|PubMed:21159175};
DE EC=1.1.5.12 {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:21159175};
DE AltName: Full=D-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000303|PubMed:21159175};
DE Short=D-LDH {ECO:0000255|HAMAP-Rule:MF_02092};
GN Name=dld {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000303|PubMed:21159175};
GN OrderedLocusNames=Cgl0901 {ECO:0000312|EMBL:BAB98294.1};
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=21159175; DOI=10.1186/1471-2180-10-321;
RA Kato O., Youn J.W., Stansen K.C., Matsui D., Oikawa T., Wendisch V.F.;
RT "Quinone-dependent D-lactate dehydrogenase Dld (Cg1027) is essential for
RT growth of Corynebacterium glutamicum on D-lactate.";
RL BMC Microbiol. 10:321-321(2010).
CC -!- FUNCTION: Catalyzes the oxidation of D-lactate to pyruvate. Has also
CC weak activity with L-lactate and DL-2-hydroxybutyrate. Electrons
CC derived from D-lactate oxidation enter the electron transport chain.
CC Essential for growth with D-lactate as sole carbon and energy source.
CC {ECO:0000269|PubMed:21159175}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lactate + a quinone = a quinol + pyruvate;
CC Xref=Rhea:RHEA:51468, ChEBI:CHEBI:15361, ChEBI:CHEBI:16004,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.1.5.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02092,
CC ECO:0000269|PubMed:21159175};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02092,
CC ECO:0000269|PubMed:21159175};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.62 mM for D-lactate {ECO:0000269|PubMed:21159175};
CC Vmax=73.5 umol/min/mg enzyme {ECO:0000269|PubMed:21159175};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:21159175};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:21159175};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02092};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_02092};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_02092}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:21159175}.
CC -!- DISRUPTION PHENOTYPE: Inactivation results in the loss of the ability
CC to grow with D-lactate. {ECO:0000269|PubMed:21159175}.
CC -!- SIMILARITY: Belongs to the quinone-dependent D-lactate dehydrogenase
CC family. {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000305}.
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DR EMBL; BA000036; BAB98294.1; -; Genomic_DNA.
DR RefSeq; NP_600129.1; NC_003450.3.
DR RefSeq; WP_011013960.1; NC_006958.1.
DR AlphaFoldDB; Q8NRY8; -.
DR SMR; Q8NRY8; -.
DR STRING; 196627.cg1027; -.
DR KEGG; cgl:Cgl0901; -.
DR PATRIC; fig|196627.13.peg.886; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_034094_0_0_11; -.
DR OMA; YEHHLML; -.
DR BRENDA; 1.1.5.10; 960.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0102029; F:D-lactate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0019516; P:lactate oxidation; IEA:UniProtKB-UniRule.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 3.30.1370.20; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.610; -; 2.
DR HAMAP; MF_02092; DLDH_Dld; 1.
DR InterPro; IPR016172; D-lactate_DH_C-sub1.
DR InterPro; IPR016173; D-lactate_DH_C-sub2.
DR InterPro; IPR012256; D_lactate_DH.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR015409; Lactate_DH_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF09330; Lact-deh-memb; 1.
DR PIRSF; PIRSF000101; D-lactate_dh; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW Cell membrane; FAD; Flavoprotein; Membrane; Oxidoreductase; Quinone;
KW Reference proteome.
FT CHAIN 1..571
FT /note="Quinone-dependent D-lactate dehydrogenase"
FT /id="PRO_0000441706"
FT DOMAIN 44..273
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
FT BINDING 78..82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
FT BINDING 86..87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
FT BINDING 145
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
FT BINDING 162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
FT BINDING 263
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
SQ 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
