NUOL_STRCO
ID NUOL_STRCO Reviewed; 654 AA.
AC Q9XAR5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 121.
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; OrderedLocusNames=SCO4573; ORFNames=SCD16A.10c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC reaction to proton translocation (for every two electrons transferred,
CC four hydrogen ions are translocated across the cytoplasmic membrane),
CC and thus conserves the redox energy in a proton gradient (By
CC similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR EMBL; AL939120; CAB44520.1; -; Genomic_DNA.
DR PIR; T34613; T34613.
DR RefSeq; NP_628735.1; NC_003888.3.
DR RefSeq; WP_003974373.1; NZ_VNID01000017.1.
DR AlphaFoldDB; Q9XAR5; -.
DR SMR; Q9XAR5; -.
DR STRING; 100226.SCO4573; -.
DR GeneID; 1100013; -.
DR KEGG; sco:SCO4573; -.
DR PATRIC; fig|100226.15.peg.4645; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_6_0_11; -.
DR InParanoid; Q9XAR5; -.
DR OMA; LIGFWQH; -.
DR PhylomeDB; Q9XAR5; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
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 Cell membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..654
FT /note="NADH-quinone oxidoreductase subunit L"
FT /id="PRO_0000118224"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 455..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 69226 MW; 0803637FAF6A2B24 CRC64;
MENLIALLVA APLLGAVVLL CGGRRLDRVG HWIGTLLAAV SFVLGVVLFA DLLGSGAEDR
TLTQHLFSWI PVEGFQADVA FRLDQLSMTF VLLITGVGSL IHLYSVAYME HDERRRRFFG
YLNLFLAAML ILVLADNYLL LYVGWEGVGL ASYLLIGFWQ HKPSAATAAK KAFLVNRVGD
MGLSIGIMLM FLWFGTFAFG PVLGGHGEAG LAAGADEGKL TAIALMLLLA ACGKSAQVPL
QSWLGDAMEG PTPVSALIHA ATMVTAGVYL IVRSGAIFNG APDAQLVVTI VGAVTLLFGA
IVGCAKDDIK KALAGSTMSQ IGYMVLAAGL GPIGYVFAIM HLVTHGFFKA GLFLGAGSVM
HGMNDEVDMR RYGGLRKYMP VTFVTFGLGY LAIIGFPGLS GFFSKDKIIE AAFAKGGTEG
WILGACALLG AAITAYYMTR VMLMTFFGEE RWRNAPTPSP AKPDVEPAAE TRGTYEPPHP
HESPGLMTIP MIVLAVGSVG AGAFFSIGDR FMHWLEPITG HSHGDSPISA GAVTGATVAC
MVIGVAVAWA QYGRRPVPAV APRGSLLTRA ARRDLLQDDF NHVVLVRGGE HLTRSLVYVD
HTVVDGVVNG TAASVGGLSG RMRRLQNGFA RSYAVSMFGG AALLVAATLL MRAV
