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NU2M_RHIOR
ID   NU2M_RHIOR              Reviewed;         523 AA.
AC   Q3T4F3;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000250|UniProtKB:Q35140};
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 2 {ECO:0000312|EMBL:AAW49463.1};
GN   Name=ND2 {ECO:0000250|UniProtKB:Q35140};
GN   Synonyms=NAD2 {ECO:0000312|EMBL:AAW49463.1};
OS   Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OG   Mitochondrion {ECO:0000312|EMBL:AAW49463.1}.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=64495;
RN   [1] {ECO:0000312|EMBL:AAW49463.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 148428 {ECO:0000312|EMBL:AAW49463.1};
RX   PubMed=15689432; DOI=10.1093/nar/gki199;
RA   Seif E., Leigh J., Liu Y., Roewer I., Forget L., Lang B.F.;
RT   "Comparative mitochondrial genomics in zygomycetes: bacteria-like RNase P
RT   RNAs, mobile elements, and a close source of the group I intron invasion in
RT   angiosperms.";
RL   Nucleic Acids Res. 33:734-744(2005).
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|UniProtKB:Q35140}.
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
CC       {ECO:0000250|UniProtKB:P03892}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P03892}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000255}.
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DR   EMBL; AY863212; AAW49463.1; -; Genomic_DNA.
DR   RefSeq; YP_203296.1; NC_006836.1.
DR   AlphaFoldDB; Q3T4F3; -.
DR   SMR; Q3T4F3; -.
DR   GeneID; 3260146; -.
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   HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR   InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   TIGRFAMs; TIGR01770; NDH_I_N; 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..523
FT                   /note="NADH-ubiquinone oxidoreductase chain 2"
FT                   /id="PRO_0000398813"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        490..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   523 AA;  57145 MW;  587869A30B88779B CRC64;
     MVLFGVLTMI LAIALFSLRI PAIYFNRITI ILLLFSALLS YNSLYMNNIG SGVGVFGGLF
     QVTTITQSID VFIYLLGALV LLLSEKANRA NTLSFNKLNS TLVNKSKGLS VLAEYPLIAL
     FSVLGMSSLI SSSDLISMFL SIELQSFAVY ILATIYRESE SATSAGLKYF LLGSLSSALI
     LLGSSLLYSF TGLTSFEGLY MLCSTTETNT AIEISVLLIM VGLLFKVSAA PFHNWAPDVY
     DGVPTVVTTW LTTMPKIAFL VFILEFQGFT QLANWSSWTN LLLISSLLSL LIGTIGGLAQ
     YRIKRLLTYS TISHVGFLLL ALAINNEESV ESFLFYLIQY SLTNINVFFI LVAFGYLLGS
     KGLSIYSPIQ LINQLKGQFK VNPLLGLSLA ICLFSMAGIP PLVGFFGKQM VLYAATHNGN
     FFLAFVAILV SVVSAAYYLR IIKVIHFDPV PAPSALSLIK TTEISSDLNV TETNNSLEGS
     SEELSTSSSL VIATITLLLI FFIINPTPLL NSVHLITLNL FYW
 
 
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