NU5M_ASCSU
ID NU5M_ASCSU Reviewed; 547 AA.
AC P24884;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 5;
GN Name=ND5;
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OG Mitochondrion.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Body wall muscle, and Egg;
RX PubMed=1551572; DOI=10.1093/genetics/130.3.471;
RA Okimoto R., Macfarlane J.L., Clary D.O., Wolstenholme D.R.;
RT "The mitochondrial genomes of two nematodes, Caenorhabditis elegans and
RT Ascaris suum.";
RL Genetics 130:471-498(1992).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) that is believed to belong to the
CC minimal assembly required for catalysis. Complex I functions in the
CC transfer of electrons from NADH to the respiratory chain. The immediate
CC electron acceptor for the enzyme is believed to be ubiquinone (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR EMBL; X54253; CAA38174.1; -; Genomic_DNA.
DR PIR; S26025; S26025.
DR RefSeq; NP_006952.2; NC_001327.1.
DR AlphaFoldDB; P24884; -.
DR SMR; P24884; -.
DR GeneID; 807668; -.
DR CTD; 4540; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR PANTHER; PTHR42829; PTHR42829; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
PE 3: Inferred from homology;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..547
FT /note="NADH-ubiquinone oxidoreductase chain 5"
FT /id="PRO_0000118063"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 547 AA; 62971 MW; 53A149DE452AE672 CRC64;
MDISIFLMVF LLFCVSLFLI FFVSCVKLSF FFVEWDFLSF KISVYFNSIM FSLILLLVTI
SVLVFSTYYL SGELNFNYYY FMLLVFVGSM FSLIFSSGCF SMLVSWDLLG ISSFFLVLFY
NNWDSCSGAM NTVLTNRLGD FFLFVFFSST IFSSYYFLSL SFFCWLSSLM LLLASFTKSA
QFPFSGWLPK AMSAPTPISS LVHSSTLVTA GLVLIMNFSE MILNKDVIMI IMVVGVFTMF
FSSMAALVEE DLKKVVALST LSQMGFSMLT VGIGLSFVSF IHLLSHALFK SCLFMQVGYL
IHCSLGQQDG RNYSNLGNVP YFIQLQLLVT LFCLCGLVFS SGAVSKDYIL EFFFSNFFMV
VFACMFFFSV FLTFGYSYRL WKGFFMSFSR PVFCFSSSVV MNFLSLLLVL FSIFFIWWMN
FNMLCMPCLF LYVDFFVPLF FVVMIMVVGF LCVKLLLKEF VYKFLVDFFA KGWVYGLKNY
KFFDLFLGGI NSLGVTFFSF TGFWSNSYMK SLYFNSVVIV LVLFFFLVWG CILSLKYALC
KRMILAL