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D-lactate dehydrogenase (acceptor) (EC 1.1.99.6)

 DLD_ARCFU               Reviewed;         443 AA.
O29853;
29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 88.
RecName: Full=D-lactate dehydrogenase (acceptor) {ECO:0000305};
EC=1.1.99.6 {ECO:0000269|PubMed:10601217};
Name=dld {ECO:0000303|PubMed:10601217};
OrderedLocusNames=AF_0394 {ECO:0000312|EMBL:AAB90839.1};
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM
9628 / NBRC 100126).
Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
Archaeoglobaceae; Archaeoglobus.
NCBI_TaxID=224325 {ECO:0000312, ECO:0000312|EMBL:AAB90839.1};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126
{ECO:0000312};
PubMed=9389475; DOI=10.1038/37052;
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
Woese C.R., Venter J.C.;
"The complete genome sequence of the hyperthermophilic, sulphate-
reducing archaeon Archaeoglobus fulgidus.";
Nature 390:364-370(1997).
[2]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=10601217;
Reed D.W., Hartzell P.L.;
"The Archaeoglobus fulgidus D-lactate dehydrogenase is a Zn(2+)
flavoprotein.";
J. Bacteriol. 181:7580-7587(1999).
[3]
SUBCELLULAR LOCATION, TOPOLOGY, AND INDUCTION.
PubMed=15803647; DOI=10.1155/2002/297264;
Pagala V.R., Park J., Reed D.W., Hartzell P.L.;
"Cellular localization of D-lactate dehydrogenase and NADH oxidase
from Archaeoglobus fulgidus.";
Archaea 1:95-104(2002).
-!- FUNCTION: Converts D-lactate to pyruvate. Cannot use NAD(+),
cytochrome C, methylene blue or dimethylnaphthoquinone as
acceptors. Active in vitro with artificial electron acceptors such
as 2,6-dichlorophenolindophenol, but the physiological acceptor is
not yet known. {ECO:0000269|PubMed:10601217}.
-!- CATALYTIC ACTIVITY: (R)-lactate + acceptor = pyruvate + reduced
acceptor. {ECO:0000269|PubMed:10601217}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:10601217};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:10601217};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=150 uM for D-lactate {ECO:0000269|PubMed:10601217};
Temperature dependence:
Optimum temperature is 90 degrees Celsius.
{ECO:0000269|PubMed:10601217};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15803647};
Multi-pass membrane protein {ECO:0000303|PubMed:15803647}.
Note=Extracellular part of the protein faces the S-layer.
{ECO:0000269|PubMed:15803647}.
-!- INDUCTION: Constitutively expressed.
{ECO:0000269|PubMed:15803647}.
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EMBL; AE000782; AAB90839.1; -; Genomic_DNA.
PIR; B69299; B69299.
RefSeq; WP_010877901.1; NC_000917.1.
ProteinModelPortal; O29853; -.
SMR; O29853; -.
STRING; 224325.AF0394; -.
EnsemblBacteria; AAB90839; AAB90839; AF_0394.
GeneID; 1483609; -.
KEGG; afu:AF_0394; -.
eggNOG; arCOG00337; Archaea.
eggNOG; COG0277; LUCA.
KO; K21836; -.
OMA; GQGFEWA; -.
OrthoDB; POG093Z03DL; -.
BRENDA; 1.1.99.6; 414.
Proteomes; UP000002199; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0047809; F:D-2-hydroxy-acid dehydrogenase activity; IDA:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
Gene3D; 1.10.45.10; -; 1.
Gene3D; 3.30.43.10; -; 1.
Gene3D; 3.30.465.10; -; 1.
InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
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; IPR004113; FAD-linked_oxidase_C.
InterPro; IPR006094; Oxid_FAD_bind_N.
InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
Pfam; PF02913; FAD-oxidase_C; 1.
Pfam; PF01565; FAD_binding_4; 1.
SUPFAM; SSF55103; SSF55103; 1.
SUPFAM; SSF56176; SSF56176; 1.
PROSITE; PS51387; FAD_PCMH; 2.
1: Evidence at protein level;
Cell membrane; Complete proteome; FAD; Flavoprotein; Membrane;
Oxidoreductase; Reference proteome; Transmembrane;
Transmembrane helix; Zinc.
CHAIN 1 443 D-lactate dehydrogenase (acceptor).
/FTId=PRO_0000430704.
TOPO_DOM 1 182 Extracellular.
{ECO:0000303|PubMed:15803647}.
TRANSMEM 183 203 Helical. {ECO:0000303|PubMed:15803647}.
TOPO_DOM 204 383 Cytoplasmic.
{ECO:0000303|PubMed:15803647}.
TRANSMEM 384 404 Helical. {ECO:0000303|PubMed:15803647}.
TOPO_DOM 405 443 Extracellular.
{ECO:0000303|PubMed:15803647}.
DOMAIN 32 209 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
SEQUENCE 443 AA; 48487 MW; 0060B82920BA478E CRC64;
MSWIDELSKI VEVFPPSDAY RFDETPPLVA PRAAENFVVV KPSNSEEVSA ILKFANEKSI
PVFMRGGGTG LSGGAVPTEE GIVLSTEKMT ELEVDADNRV AICGAGVTLK QLDDAAFRHG
LSFPPHPGAE TATVGGMIAT NAGGVRALKY GTMRNYVLSL EAVLADGRII NVGGKTIKNS
SGYSLLHLLV GSEGTLAVIT KATIRLFPQM RDMTVLAIPF PTMEDAMNCV VEVARKMLPM
ALEFMEKRAV EIGEKVSGER WVSREGEAHL LMVFESFDEA EEAAKIAQSL GAIDVYAATT
KKDQDRLLKV RGMIYEGLRK EVIEVLDACV PPAKIAEYWR RSNELAEEYG IELITYGHAG
DGNVHQHPLV YEGWEKSYFE FRKSLLSLAV SLGGVISGEH GIGAVKLSEL EELFPEQFEL
MRQIKLLFDP KNILNPGKVV RKL


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