NU5M_CRYPA
ID NU5M_CRYPA Reviewed; 656 AA.
AC Q8HHD2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5;
DE EC=7.1.1.2;
GN Name=ND5;
OS Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Cryphonectriaceae;
OC Cryphonectria-Endothia species complex; Cryphonectria.
OX NCBI_TaxID=5116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14599889; DOI=10.1016/j.fgb.2003.08.003;
RA Gobbi E., Firrao G., Carpanelli A., Locci R., Van Alfen N.K.;
RT "Mapping and characterization of polymorphism in mtDNA of Cryphonectria
RT parasitica: evidence of the presence of an optional intron.";
RL Fungal Genet. Biol. 40:215-224(2003).
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; AF456838; AAO14099.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8HHD2; -.
DR SMR; Q8HHD2; -.
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..656
FT /note="NADH-ubiquinone oxidoreductase chain 5"
FT /id="PRO_0000118084"
FT TRANSMEM 5..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..653
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 656 AA; 72601 MW; 35C99E836E257DBA CRC64;
MYLSIIILPV LGSIVAGFFG RKLGVRGAQI ITCSCVIVTT ILALLAWVEV GFNNIPVTIN
LFRWIDSEWF NIIWGFQFDS LTVSMLLPVL IISSLVHIYS ISYMSGDPHN QRFFSYLSLF
TFMMIILVTG NNYLLMFVGW EGVGVCSYLL VSFWFTRIAA NQSSISAFLT NRVGDCFLTI
GMFAILWSLG NLDYATVFSL APYINENIIT IIGICLVIGA MAKSSQVGLH VWLPMAMEGP
TPVSALIHAA TMVTAGVYLL MRSSPLIEYS STVLLICLWL GAITTVFSSL VGLFQQDIKK
VIAYSTMSQL GLMVVAIGLS SYNIALFHLV NHAFYKAALF LGAGSIIHAV ADNQDFRKYG
GLREFLPLTY SIILIASLSL AAFPFLTGFY SKDLILESAF GQFTFSGVSV YAISTIGAIF
TTLYSVKVIY LTFLANPNGS LMTVRHAHEG DIFLTLPLVI LAIFSIFFGY LTKDIFIGLG
SSFFVDNSLY VHPVHEILID TEFGVPTVFK ILPFIFTVLF SILAILLSEF IPGSVFNFKL
SRFGYNLFGF FNQRFLIEMF YNNYITNLVL TLGSQTTKVL DKGSVELIGP FGLEKGLMNF
SKSLTKLSTG VVTSYALYIL LGLISFIIIL YLSQISSSLI VLLIILTLFS LNFNKQ
