ID A0A0C9MIH9_9FUNG Unreviewed; 622 AA.
AC A0A0C9MIH9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=NDI, mitochondrial NADH dehydrogenase {ECO:0000313|EMBL:GAN10651.1};
GN ORFNames=MAM1_0381d10196 {ECO:0000313|EMBL:GAN10651.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN10651.1};
RN [1] {ECO:0000313|EMBL:GAN10651.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN10651.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004137}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004137}; Intermembrane side
CC {ECO:0000256|ARBA:ARBA00004137}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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DR EMBL; DF836670; GAN10651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9MIH9; -.
DR STRING; 91626.A0A0C9MIH9; -.
DR OrthoDB; 48029at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR Gene3D; 3.50.50.100; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR43706:SF50; NADH DEHYDROGENASE (UBIQUINONE)-RELATED; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 437..472
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 478..513
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 622 AA; 70181 MW; D65235F2CA463090 CRC64;
MFSRSLLATS KSLPRNSNVR LIRRAFLGSS SSSKVPNAWI GPKLKRLFLV GGAAGAVGSF
AYYLSQDQER VVDVFGESEH VPYLALHPER GGAKGLPISK YYIDDNTEHE NRKERVVILG
SGWGAISVIK NLDKDKYNVT VVSDNNYFLF TPLLPSATVG TLELRSLIEP VRKITARIKA
HFVEGRAADI DLENKLVEVQ GCNGDENFYV PYDKLIVAVG ATSMTHGVEG IENTVRLKTI
QDAMRIRHLV TENVEKACLP TTSPEERKRL LSFVVCGGGP TGVEFAAEMS DWINEDLVKW
FPKLVREDIS IHIIQSRDHI LNTFDSKISE YAEKRFDREH VNVITNARVA RIEDKEVIYK
LKSSDPNAEP VIQKLPYGLC LWSTGIAMTP FAQHLTQKLP EQAHKRVLTT DNYLHLRGLN
DDSIFALGDC ASIENPNLLE HIMEFFQEAD SDKDGSLSLN EFLAICNAMK ERFPLTEEHL
ANLEHKFRKY DSNHSGTLEI DEMKAMLKDV DSKLTNLPAT AQVASQQGQY LAKYLNTLYE
KDESSTKQTV GPFRYNHLGT LAYLGNTAVG DFKWGYQMIG GLWALYLWRS VYWSEQVSMR
TRMNLSLDWT RCAIWGRDIS TV
//