ID H8KMD4_SOLCM Unreviewed; 635 AA.
AC H8KMD4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Proton-translocating NADH-quinone oxidoreductase, chain L {ECO:0000313|EMBL:AFD08729.1};
GN OrderedLocusNames=Solca_3729 {ECO:0000313|EMBL:AFD08729.1};
OS Solitalea canadensis (strain ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB
OS 12057 / USAM 9D) (Flexibacter canadensis).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Solitalea.
OX NCBI_TaxID=929556 {ECO:0000313|EMBL:AFD08729.1, ECO:0000313|Proteomes:UP000007590};
RN [1] {ECO:0000313|Proteomes:UP000007590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D
RC {ECO:0000313|Proteomes:UP000007590};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Schroeder M., Kopitz M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Solitalea canadensis DSM 3403.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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 complex I subunit 5 family.
CC {ECO:0000256|ARBA:ARBA00008200}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003349; AFD08729.1; -; Genomic_DNA.
DR RefSeq; WP_014681952.1; NC_017770.1.
DR AlphaFoldDB; H8KMD4; -.
DR STRING; 929556.Solca_3729; -.
DR KEGG; scn:Solca_3729; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_6_0_10; -.
DR OrthoDB; 9807568at2; -.
DR Proteomes; UP000007590; 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:UP000007590};
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 5..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 511..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 613..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..117
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 135..420
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 447..579
FT /note="NADH:ubiquinone/plastoquinone oxidoreductase
FT chloroplast chain 5 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01010"
SQ SEQUENCE 635 AA; 69177 MW; 8ECA1D0802F16192 CRC64;
MTEQLAWLIP VLPLIGFLIN GLGYKKNPKG LVGLVGCATV LGSFILSILV FFDIKANGAK
TIDLYDWISV GSLHIPFSFL VDQLTSIMLL IITGVGFLIH VYSTGYMHDD EGYGKYFAYL
NLFVFFMLLL VMGSNYVIMF IGWEGVGLCS YLLIGFWFKK TEYASAAKKA FVMNRIGDLG
FLLGIFMLFS TFGSTSFADI FPKAEGASVT VLTTITLLLF VGAMGKSAQL PLFTWLPDAM
AGPTPVSALI HAATMVTAGI YMIARSNVLY VLSPISMAVV AGVGLATAIF AAIIALTQND
IKKVLAYSTV SQLGYMFLGL GVGAFTGAFF HVMTHAFFKA LLFLGAGSVI HAMGGEQDMR
KMGGLKKHLP ITWITMLMGT IAIAGIPPFS GFFSKDEILA HAYEVSPTIW IIGVGGALLT
AFYMFRMFFL TFNGTFRGTD HQHHHLHESP ASMTIPLIVL AVLSVVGGFV GVPEALGGSH
MLNEFLSPVF ARSTEIMQAS HHGHLSHSTE YALIAASVLG VVISILYAYF VYVKKATIPA
ADIARRVGIE KASYNKFYVD EIYNAVFTRP LDNLSQLFYR IVDKSVIDGV VNGFGQLTQW
GADKIRLIQT GNIGSYLFMM VVGIILILVF NFLIF
//