ID DLD_ARCFU Reviewed; 443 AA.
AC O29853;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=D-lactate dehydrogenase {ECO:0000303|PubMed:10601217};
DE EC=1.1.99.6 {ECO:0000269|PubMed:10601217};
GN Name=dld {ECO:0000303|PubMed:10601217};
GN OrderedLocusNames=AF_0394 {ECO:0000312|EMBL:AAB90839.1};
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10601217; DOI=10.1128/jb.181.24.7580-7587.1999;
RA Reed D.W., Hartzell P.L.;
RT "The Archaeoglobus fulgidus D-lactate dehydrogenase is a Zn(2+)
RT flavoprotein.";
RL J. Bacteriol. 181:7580-7587(1999).
RN [3]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND INDUCTION.
RX PubMed=15803647; DOI=10.1155/2002/297264;
RA Pagala V.R., Park J., Reed D.W., Hartzell P.L.;
RT "Cellular localization of D-lactate dehydrogenase and NADH oxidase from
RT Archaeoglobus fulgidus.";
RL Archaea 1:95-104(2002).
CC -!- FUNCTION: Catalyzes the dehydrogenation of (R)-lactate (D-lactate) to
CC pyruvate. Is likely involved in the utilization of D-lactate as a sole
CC source for both carbon and electrons for dissimilatory sulfate
CC reduction. Cannot use L-lactate as substrate, and NAD(+), horse
CC cytochrome c, methylene blue or dimethylnaphthoquinone as acceptors.
CC Active in vitro with artificial electron acceptors such as 2,6-
CC dichlorophenolindophenol (DCPIP); the physiological acceptor is not
CC known, but potential acceptors include cytochromes or quinones.
CC {ECO:0000269|PubMed:10601217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lactate + A = AH2 + pyruvate; Xref=Rhea:RHEA:15089,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:16004,
CC ChEBI:CHEBI:17499; EC=1.1.99.6;
CC Evidence={ECO:0000269|PubMed:10601217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15090;
CC Evidence={ECO:0000305|PubMed:10601217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10601217};
CC Note=Binds 1 FAD non-covalently per subunit.
CC {ECO:0000269|PubMed:10601217};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10601217};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000269|PubMed:10601217};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=150 uM for D-lactate {ECO:0000269|PubMed:10601217};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:10601217};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius.
CC {ECO:0000269|PubMed:10601217};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15803647};
CC Multi-pass membrane protein {ECO:0000303|PubMed:15803647}.
CC Note=Extracellular part of the protein faces the S-layer.
CC {ECO:0000269|PubMed:15803647}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:15803647}.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000305}.
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DR EMBL; AE000782; AAB90839.1; -; Genomic_DNA.
DR PIR; B69299; B69299.
DR RefSeq; WP_010877901.1; NC_000917.1.
DR AlphaFoldDB; O29853; -.
DR SMR; O29853; -.
DR STRING; 224325.AF_0394; -.
DR PaxDb; 224325-AF_0394; -.
DR EnsemblBacteria; AAB90839; AAB90839; AF_0394.
DR GeneID; 1483609; -.
DR KEGG; afu:AF_0394; -.
DR eggNOG; arCOG00337; Archaea.
DR HOGENOM; CLU_017779_9_2_2; -.
DR OrthoDB; 26910at2157; -.
DR PhylomeDB; O29853; -.
DR BRENDA; 1.1.99.6; 414.
DR SABIO-RK; O29853; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047809; F:D-2-hydroxy-acid dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW Cell membrane; FAD; Flavoprotein; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..443
FT /note="D-lactate dehydrogenase"
FT /id="PRO_0000430704"
FT TOPO_DOM 1..182
FT /note="Extracellular"
FT /evidence="ECO:0000303|PubMed:15803647"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000303|PubMed:15803647"
FT TOPO_DOM 204..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000303|PubMed:15803647"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000303|PubMed:15803647"
FT TOPO_DOM 405..443
FT /note="Extracellular"
FT /evidence="ECO:0000303|PubMed:15803647"
FT DOMAIN 32..209
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ 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
//
