ID Q0C1N1_HYPNA Unreviewed; 553 AA.
AC Q0C1N1;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=D-lactate dehydrogenase {ECO:0000256|PIRNR:PIRNR000101};
DE EC=1.1.5.12 {ECO:0000256|PIRNR:PIRNR000101};
GN Name=dld {ECO:0000313|EMBL:ABI78065.1};
GN OrderedLocusNames=HNE_1654 {ECO:0000313|EMBL:ABI78065.1};
OS Hyphomonas neptunium (strain ATCC 15444).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hyphomonas.
OX NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI78065.1, ECO:0000313|Proteomes:UP000001959};
RN [1] {ECO:0000313|EMBL:ABI78065.1, ECO:0000313|Proteomes:UP000001959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI78065.1,
RC ECO:0000313|Proteomes:UP000001959};
RX PubMed=16980487; DOI=10.1128/JB.00111-06;
RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA Ward N.L.;
RT "Comparative genomic evidence for a close relationship between the
RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT crescentus.";
RL J. Bacteriol. 188:6841-6850(2006).
CC -!- FUNCTION: Catalyzes the oxidation of D-lactate to pyruvate.
CC {ECO:0000256|PIRNR:PIRNR000101}.
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:0000256|PIRNR:PIRNR000101};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRNR:PIRNR000101, ECO:0000256|PIRSR:PIRSR000101-1};
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DR EMBL; CP000158; ABI78065.1; -; Genomic_DNA.
DR RefSeq; WP_011646662.1; NC_008358.1.
DR AlphaFoldDB; Q0C1N1; -.
DR STRING; 228405.HNE_1654; -.
DR KEGG; hne:HNE_1654; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_034094_0_0_5; -.
DR Proteomes; UP000001959; Chromosome.
DR GO; GO:0005886; C: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:InterPro.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.610; D-lactate dehydrogenase, cap domain, subdomain 1; 2.
DR Gene3D; 3.30.1370.20; D-lactate dehydrogenase, cap domain, subdomain 2; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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 PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF3; QUINONE-DEPENDENT D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF09330; Lact-deh-memb; 1.
DR PIRSF; PIRSF000101; D-lactate_dh; 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 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000101};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000101};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000101,
KW ECO:0000313|EMBL:ABI78065.1}; Quinone {ECO:0000256|PIRNR:PIRNR000101};
KW Reference proteome {ECO:0000313|Proteomes:UP000001959}.
FT DOMAIN 28..255
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT BINDING 70..71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 128
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 145
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 242
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 247
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000101-1"
SQ SEQUENCE 553 AA; 60507 MW; BF8A2FE02D7C5645 CRC64;
MISDAALIRE LKVIVGSGHV NVRDDRRASG KPVTFVRPRT LVEVWRVARA SVRAGRIILM
RAGGTSLTGG SAPNGAYDRG VVVINTMRLK GIHMLNAGAQ VLCLPGTTLF ELERELRPLQ
REPHSELGST WLGASVIGGV CNNSGGAQVR RGPAYTEAAL YAHVDETGEL RLVNELGMDL
GRDPEEQLES LERGEFVRVL HDMHERACSA HGFVERVRDV DAPSPARFNA DPRYLKGASG
SAGRLIVFAV RLDTFPRAAN TQVFHVATDD AGVLSDVRRR MLGQAALVPI SAEYMHRDTF
RMAEREGKDL LLAVRTAGAD RLPFLFGFKA GVDGVARWLG FGRACLTDRL LQAVGRLAPP
QLSETLRQMG EQYAHHLFLK VEADQAAGVR ALLADVVPAL KGACHECSPA EGRQVFLHRF
AATGAAARHA AMSRGKAGAV VELDVALRRN DKAWWYVLPD HLKGMVEHTL VHGHFFCHVF
QQDYILKKGA DAAAFRRGMA AHYEARGAEC PAEHNVGHRH KAKPALAAFY RKLDPTNTLN
PGIGRTSRDK NWK
//
