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Database: UniProt/TrEMBL
Entry: Q4QJU3_HAEI8
LinkDB: Q4QJU3_HAEI8
Original site: Q4QJU3_HAEI8 
ID   Q4QJU3_HAEI8            Unreviewed;       564 AA.
AC   Q4QJU3;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   28-MAR-2018, entry version 85.
DE   RecName: Full=Quinone-dependent D-lactate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02092};
DE            EC=1.1.5.12 {ECO:0000256|HAMAP-Rule:MF_02092};
DE   AltName: Full=D-lactate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02092};
DE            Short=D-LDH {ECO:0000256|HAMAP-Rule:MF_02092};
GN   Name=dld {ECO:0000256|HAMAP-Rule:MF_02092,
GN   ECO:0000313|EMBL:AAX88704.1};
GN   OrderedLocusNames=NTHI1952 {ECO:0000313|EMBL:AAX88704.1};
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310 {ECO:0000313|EMBL:AAX88704.1, ECO:0000313|Proteomes:UP000002525};
RN   [1] {ECO:0000313|EMBL:AAX88704.1, ECO:0000313|Proteomes:UP000002525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP {ECO:0000313|EMBL:AAX88704.1,
RC   ECO:0000313|Proteomes:UP000002525};
RX   PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S.Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable
RT   Haemophilus influenzae: comparative study with H. influenzae serotype
RT   d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
CC   -!- FUNCTION: Catalyzes the oxidation of D-lactate to pyruvate.
CC       {ECO:0000256|HAMAP-Rule:MF_02092, ECO:0000256|PIRNR:PIRNR000101}.
CC   -!- CATALYTIC ACTIVITY: (R)-lactate + a quinone = pyruvate + a quinol.
CC       {ECO:0000256|HAMAP-Rule:MF_02092, ECO:0000256|PIRNR:PIRNR000101}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02092, ECO:0000256|PIRNR:PIRNR000101,
CC         ECO:0000256|PIRSR:PIRSR000101-1};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02092}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_02092}; Cytoplasmic side {ECO:0000256|HAMAP-
CC       Rule:MF_02092}.
CC   -!- SIMILARITY: Belongs to the quinone-dependent D-lactate
CC       dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_02092}.
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DR   EMBL; CP000057; AAX88704.1; -; Genomic_DNA.
DR   RefSeq; WP_011272721.1; NC_007146.2.
DR   ProteinModelPortal; Q4QJU3; -.
DR   EnsemblBacteria; AAX88704; AAX88704; NTHI1952.
DR   KEGG; hit:NTHI1952; -.
DR   HOGENOM; HOG000122232; -.
DR   KO; K03777; -.
DR   OMA; RDRYEHH; -.
DR   OrthoDB; POG091H0GWB; -.
DR   Proteomes; UP000002525; 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:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016901; F:oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
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; 3.30.70.610; -; 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_2.
DR   InterPro; IPR036318; FAD-bd_2-like_sf.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
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   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02092};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_02092};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002525};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_02092, ECO:0000256|PIRNR:PIRNR000101,
KW   ECO:0000256|PIRSR:PIRSR000101-1, ECO:0000256|SAAS:SAAS00990849};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02092,
KW   ECO:0000256|PIRNR:PIRNR000101, ECO:0000256|SAAS:SAAS00990758};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_02092};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02092,
KW   ECO:0000256|PIRNR:PIRNR000101, ECO:0000313|EMBL:AAX88704.1};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_02092,
KW   ECO:0000256|PIRNR:PIRNR000101}.
FT   DOMAIN       36    207       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
FT   NP_BIND      70     79       FAD. {ECO:0000256|PIRSR:PIRSR000101-1}.
FT   NP_BIND      70     74       FAD. {ECO:0000256|HAMAP-Rule:MF_02092}.
FT   NP_BIND      78     79       FAD. {ECO:0000256|HAMAP-Rule:MF_02092}.
FT   BINDING     137    137       FAD. {ECO:0000256|PIRSR:PIRSR000101-1}.
FT   BINDING     137    137       FAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02092}.
FT   BINDING     144    144       FAD. {ECO:0000256|HAMAP-Rule:MF_02092,
FT                                ECO:0000256|PIRSR:PIRSR000101-1}.
FT   BINDING     154    154       FAD. {ECO:0000256|PIRSR:PIRSR000101-1}.
FT   BINDING     154    154       FAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02092}.
FT   BINDING     251    251       FAD. {ECO:0000256|PIRSR:PIRSR000101-1}.
FT   BINDING     256    256       FAD. {ECO:0000256|PIRSR:PIRSR000101-1}.
FT   BINDING     256    256       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02092}.
SQ   SEQUENCE   564 AA;  64092 MW;  A4879692317974BA CRC64;
     MSVQQLISRL TDIVGSRYII TDPTKTEAYR SGYRFGTGNA LAVVRPATLL EFWNIVKVCV
     EHDVIVINQA ANTGLTGGST PDGNDYDRDI VVINTMRIDG IKLINNASQV ICLPGSTLNE
     LENQLKPFGR EPHSVIGSSC IGASVIGGIC NNSGGALVQR GPAYTEMALY AQLNEKGELE
     LKNHLGIDLG ETPEEILTNL QEKRYQVKDI RQDCGHGHDH YYCNYVRQVD EGSPARFNAD
     PARHYEASGC AGKLAVFAVR LDTFPLEKET AVFYIGTNQT SVLSDIRRHM LVNFEVLPIS
     GEYIHRDAFD IAAKYGKDTF WVIKKFGTHW LPKLFSLKSN VDRIGKKFFF LPQHLSDKLM
     QTVSKFIPEH LPQSLWDYRN KYEHHLIIKM GGKGIQEARE YLESYIADGS KGGYFECNAI
     ETQAAMLHRF AVASAAIRYR AIHEKEVEEI VALDVALRRN DQDWFEVLPP EIDNRIISKL
     YYGHFMCHVF HQDYIVKKGY DYEELEYEML KLLDKRGAQY PAEHNVGHLY EAKPTLRKFY
     KELDPTNSFN PGIGKTTRKK YWAE
//
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