ID Q6MA66_PARUW Unreviewed; 414 AA.
AC Q6MA66;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN ORFNames=PC_RS08675 {ECO:0000313|EMBL:CAF24533.1};
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Protochlamydia.
OX NCBI_TaxID=264201 {ECO:0000313|EMBL:CAF24533.1, ECO:0000313|Proteomes:UP000000529};
RN [1] {ECO:0000313|EMBL:CAF24533.1, ECO:0000313|Proteomes:UP000000529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25 {ECO:0000313|EMBL:CAF24533.1,
RC ECO:0000313|Proteomes:UP000000529};
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000864};
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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DR EMBL; BX908798; CAF24533.1; -; Genomic_DNA.
DR RefSeq; WP_011176354.1; NC_005861.2.
DR AlphaFoldDB; Q6MA66; -.
DR STRING; 264201.pc1809; -.
DR KEGG; pcu:PC_RS08675; -.
DR eggNOG; COG1252; Bacteria.
DR HOGENOM; CLU_021377_7_1_0; -.
DR OrthoDB; 9781621at2; -.
DR Proteomes; UP000000529; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR Gene3D; 3.50.50.100; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706:SF3; EXTERNAL NADH-UBIQUINONE OXIDOREDUCTASE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000529};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 367..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..320
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 414 AA; 46477 MW; ECA5C1981CA0424F CRC64;
MRKIIVVGGG FGGLNTVRSL KNAQVEILLI DRTNHHVFQP LLYQVATAAL SVENITTPLR
EILKNQSNVR VLMAEIEKIN LENQYIQAVD GQQFYYDDLI LAPGARHTYF GHDNWEHFAP
GLKTVADAFR IREKMLMAFE KAERCENREA VQSSLSFVII GAGPTGVEMA GSMAEFAHRT
LFKNFRSINP ANSKIYLIEE GQQILPSFPG ELANRALEDL KQLGVEVLLN TFVTQVTDQG
VYMNEKFLPA FTVVWAAGNE ASPLVKSLGV SLDKQSRVKV QPDLTIPGFT NVFVIGDAAA
VVSSKNEFLP GIAPVAIQQG HYVANLIKKN ILPSNRKPFL YWDKGMIATI GRGRAVAILG
NFKFSGFLAW LIWCFIHILY LVSFGHRLLV MIQWIFLYLF NRRQARVIIR PIQE
//
