ID C8W5B5_DESAS Unreviewed; 642 AA.
AC C8W5B5;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Proton-translocating NADH-quinone oxidoreductase, chain L {ECO:0000313|EMBL:ACV62097.1};
GN OrderedLocusNames=Dtox_1213 {ECO:0000313|EMBL:ACV62097.1};
OS Desulfofarcimen acetoxidans (strain ATCC 49208 / DSM 771 / KCTC 5769 / VKM
OS B-1644 / 5575) (Desulfotomaculum acetoxidans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfofarcimen.
OX NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV62097.1, ECO:0000313|Proteomes:UP000002217};
RN [1] {ECO:0000313|EMBL:ACV62097.1, ECO:0000313|Proteomes:UP000002217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC {ECO:0000313|Proteomes:UP000002217};
RX PubMed=21304664; DOI=10.4056/sigs.39508;
RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT (5575).";
RL Stand. Genomic Sci. 1:242-253(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000256|ARBA:ARBA00001230};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000256|ARBA:ARBA00001558};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}.
CC -!- SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit A
CC family. {ECO:0000256|ARBA:ARBA00008483}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family.
CC {ECO:0000256|ARBA:ARBA00008200}.
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DR EMBL; CP001720; ACV62097.1; -; Genomic_DNA.
DR RefSeq; WP_015756812.1; NC_013216.1.
DR AlphaFoldDB; C8W5B5; -.
DR STRING; 485916.Dtox_1213; -.
DR KEGG; dae:Dtox_1213; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_6_0_9; -.
DR OrthoDB; 9807568at2; -.
DR Proteomes; UP000002217; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR Gene3D; 1.20.5.2700; -; 1.
DR InterPro; IPR002128; NADH_UbQ_OxRdtase_chlpt_su5_C.
DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR NCBIfam; TIGR01974; NDH_I_L; 1.
DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR Pfam; PF01010; Proton_antipo_C; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
DR PRINTS; PR01435; NPOXDRDTASE5.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 33..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 505..526
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 611..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..123
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 139..431
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 438..561
FT /note="NADH:ubiquinone/plastoquinone oxidoreductase
FT chloroplast chain 5 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01010"
SQ SEQUENCE 642 AA; 70568 MW; 9AC23C2814381660 CRC64;
MVEFAMHNAW LVPLLPAIAF LIIVFLTRPW QRLSSLVCIA GMVGAFVFAA LAAYGVFTNE
EFTKHSMVYA TRWFSMPGLH IDFGIQLDPT SAMMMFMVSM VSTLIFIYAT GYMEGDPGYS
TFFAYVSLFG ASMLGLVLSS NLLQMFIFWE LVGLCSYLLI GFFTHKVSAR EAAKKAFVTC
RIADFCLLLG LLSIQIVFGT LDMVKLAEII PNFRAYTSEG ILVMIAVLVF IGPVGKSGQF
PLHVWLPDAM EGPTPVSALI HAATMVVAGV YLVGRTMFLF EQVPSVMELV AFTGAFTALF
AASIALTQRE IKRILAYSTV SQLGYMVLAL GVGSLSASMF HLWTHAFFKA LMFMGAGSVL
HALHHKADVW EMGGLLKKMP ITGWTFVVGG VAIAGIPPFA GFWSKDEILA VTLDSGHTLL
FLMAALTAFM TAFYMWRLIF LAFFGAEKPE NHPHESPWNM TLPLVVLAGL ATVGGLMGTP
WKNYWGEWIF FSGSHIHAHH GEPNYMVMIG SVVLALCGIG LAYRLYLADS EKATAKELAR
RFSGLHALSY NKFYVDELYL WINHNLVDGA AKVFYLFDLF IVDGFINALG AITKLAGDGF
RIFQTGRMQN YVLIFFLGVL VIAIVMAFSN PSSAGLILGG VK
//
