NUOL_RHOCA
ID NUOL_RHOCA Reviewed; 712 AA.
AC P50939;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=NADH-quinone oxidoreductase subunit L;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit L;
DE AltName: Full=NDH-1 subunit L;
GN Name=nuoL;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10;
RX PubMed=8566820; DOI=10.1016/0378-1119(95)00693-1;
RA Dupuis A., Peinnequin A., Chevallet M., Lunardi J., Darrouzet E.,
RA Pierrard B., Procaccio V., Issartel J.P.;
RT "Identification of five Rhodobacter capsulatus genes encoding the
RT equivalent of ND subunits of the mitochondrial NADH-ubiquinone
RT oxidoreductase.";
RL Gene 167:99-104(1995).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Dupuis A., Issartel J.P.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33303 / B10;
RA Dupuis A., Peinnequin A., Darrouzet E., Lunardi J.;
RT "Genetic disruption of the respiratory NADH-ubiquinone reductase of
RT Rhodobacter capsulatus leads to an unexpected photosynthesis-negative
RT phenotype.";
RL FEMS Microbiol. Lett. 148:107-114(1997).
RN [4]
RP SUBCELLULAR LOCATION IN CHROMATOPHORE.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=9632256; DOI=10.1046/j.1365-2958.1998.00814.x;
RA Dupuis A., Darrouzet E., Duborjal H., Pierrard B., Chevallet M.,
RA van Belzen R., Albracht S.P.J., Lunardi J.;
RT "Distal genes of the nuo operon of Rhodobacter capsulatus equivalent to the
RT mitochondrial ND subunits are all essential for the biogenesis of the
RT respiratory NADH-ubiquinone oxidoreductase.";
RL Mol. Microbiol. 28:531-541(1998).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H,
CC J, K, L, M, N constitute the membrane sector of the complex (Probable).
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000269|PubMed:9632256}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9632256}.
CC -!- DISRUPTION PHENOTYPE: No functional NADH-quinone oxidoreductase
CC complex. Cells lacking this gene have a nearly normal respiratory
CC growth phenotype on lactate, however they are unable to perform
CC anaerobic photosynthesis. It is suggested that in R.capsulatus this
CC complex may function in reverse flow under physiological conditions.
CC {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR EMBL; AF029365; AAC25003.1; -; Genomic_DNA.
DR RefSeq; WP_013067259.1; NZ_VIBE01000008.1.
DR AlphaFoldDB; P50939; -.
DR SMR; P50939; -.
DR GeneID; 31490415; -.
DR OMA; LIGFWQH; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore 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 InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR PANTHER; PTHR42829; PTHR42829; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR TIGRFAMs; TIGR01974; NDH_I_L; 1.
PE 3: Inferred from homology;
KW Membrane; NAD; Quinone; Translocase; Transmembrane; Transmembrane helix;
KW Ubiquinone.
FT CHAIN 1..712
FT /note="NADH-quinone oxidoreductase subunit L"
FT /id="PRO_0000118221"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..706
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 712 AA; 77532 MW; 3886161440079783 CRC64;
MTTIILLAPL LGALIGGFGW RLITEKGALV VTTGLLFLSC ILSWVVFLTL PAETQHIHLL
DWIRSGALDT SWGIRLDRLT AIMLIVVTTV SALVHLYSWG YMAHDENWTH HEAYKARFFA
YLSFFTFAML MLVTSDNLVQ MFFGWEGVGV ASYLLIGFYY KKPSANAAAI KAFVVNRVGD
FGFALGIMGL FFLTDSIDMD VIFASAPELA KTELHFLAWE FNAANLLAVL LFIGAMGKSA
QLFLHTWLPD AMEGPTPVSA LIHAATMVTA GVFLVCRMSP LFEYAPEAKM MVVYVGAVTA
FFAATVGLVQ NDIKRVIAYS TCSQLGYMFV AAGSGVYSVA MFHLLTHAFF KAMLFLGAGS
VIHAMHHEQD MRNYGGLRKK IPFTFAIMMI GTLAITGVGI PFFSIGGVPV GFAGYLSKDA
IIESAFASGN GFAFYVLVAA AGMTSFYSWR LIFLTFYGEA RGDHHKHDHA HESPAVMLAP
LALLAVGSVL AGMVWYHSFF GDKVASFFNL PAAAHGEAHG TEHATEGHVP EAAMTAEAAH
EAAMAGTMAM AEPAAEHAVA KAPQGAIFMA ETNHVIHDAH GVPDWVKLSP FGAMVTGFFF
AWLYYIGDKP LPGRTARALP GLYRFLLNKW YFDELFDLLF VNPAKSLGRK LWKGGDGAVI
DGAINGLALG WIPFFTRVAG RIQSGYLFHY AFAMVLGIVA LMFWVVRTGG MN
