NU5M_POLOR
ID NU5M_POLOR Reviewed; 613 AA.
AC Q95918;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 5;
GN Name=MT-ND5; Synonyms=MTND5, NADH5, ND5;
OS Polypterus ornatipinnis (Ornate bichir).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Polypteriformes; Polypteridae; Polypterus.
OX NCBI_TaxID=49895;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8913758; DOI=10.1093/genetics/144.3.1165;
RA Noack K., Zardoya R., Meyer A.;
RT "The complete mitochondrial DNA sequence of the bichir (Polypterus
RT ornatipinnis), a basal ray-finned fish: ancient establishment of the
RT consensus vertebrate gene order.";
RL Genetics 144:1165-1180(1996).
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; U62532; AAC60315.1; -; Genomic_DNA.
DR PIR; T11464; T11464.
DR RefSeq; NP_008326.1; NC_001778.1.
DR AlphaFoldDB; Q95918; -.
DR SMR; Q95918; -.
DR GeneID; 808030; -.
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; IPR010934; NADH_DH_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 PANTHER; PTHR42829; PTHR42829; 1.
DR Pfam; PF06455; NADH5_C; 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 Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..613
FT /note="NADH-ubiquinone oxidoreductase chain 5"
FT /id="PRO_0000118137"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 613 AA; 68300 MW; 62B13DD5FCFDCCE2 CRC64;
MSISQLSQMF MTCLSLTMII LILPITFSFI TKPSNKWPFQ VKNAVKLSFF VSLIPSITCL
NLNLQSFTIY YQWFSISSTK INISLQFDQY SMIFMTIALY VTWSILEFAI YYMHTDILIN
RFFKYLLTFL IAMMILVTAN NMFQLFIGWE GVGIMSFLLI GWWYGRADAN MAALQAVIYN
RVGDIGLMMT MSWLLINTNS WDIQQLFGLT KNMDTTLPAT GLLLAATGKS AQFGLHPWLP
AAMEGPTPVS ALLHSSTMVV AGIFLLIRLH PLIENNNNIL TAALCLGAIT TLFTATCALT
QNDIKKIVGF STSSQLGLMM VAIGLNQPQL AFLHICTHAF FKAMLFLCSG SIIHSLNDEQ
DIRKMGGINK TLPLTSSCLT IGSLALMGTP FLAGFFSKDA IIEAINTSHL NAWALVLTLI
ATSFTAVYSL RIIYFVLMNH PRTLPLSPVN ENNPLIANPI KRLAWGSIIA GLILCQYILP
NKTQTLTMTP MLKLTALIVS LLGLLTALEL ASMANKQIKI NPTKFTHNFS NMLGFYPHIM
HRLMSKLPLM LGQISATQMS DQLWMEKLGP KGIAHTQLLV TQKITHVHKG LIKTYLSIMM
LSIIIITIII MIT