ID   NDUS8_ARATH             Reviewed;         222 AA.
AC   Q42599;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 82.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;
DE            EC=1.6.5.3;
DE            EC=1.6.99.3;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 23 kDa subunit;
DE   AltName: Full=Complex I-23kD;
DE            Short=CI-23kD;
DE   AltName: Full=Complex I-28.5kD;
DE            Short=CI-28.5kD;
DE   Flags: Precursor;
GN   Name=TYKY; OrderedLocusNames=At1g79010;
GN   ORFNames=YUP8H12R_21, YUP8H12R.37;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. C24;
RX   MEDLINE=97188519; PubMed=9037104; DOI=10.1007/s004380050342;
RA   Schmidt-Bleek K., Heiser V., Thieck O., Brennicke A., Grohmann L.;
RT   "The 28.5-kDa iron-sulfur protein of mitochondrial complex I is
RT   encoded in the nucleus in plants.";
RL   Mol. Gen. Genet. 253:448-454(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome
RT   highlights signaling and regulatory components, provides assessment of
RT   targeting prediction programs, and indicates plant-specific
RT   mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory
CC       chain NADH dehydrogenase (Complex I) that is believed to belong to
CC       the minimal assembly required for catalysis. Complex I functions
CC       in the transfer of electrons from NADH to the respiratory chain.
CC       The immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity). May donate electrons to ubiquinone.
CC   -!- CATALYTIC ACTIVITY: NADH + ubiquinone = NAD(+) + ubiquinol.
CC   -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity).
CC   -!- SUBUNIT: Complex I is composed of about 40 different subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (Probable).
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC   -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
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DR   EMBL; X84318; CAA59061.1; -; mRNA.
DR   EMBL; AC002986; AAC17054.1; -; Genomic_DNA.
DR   EMBL; AY048241; AAK82503.1; -; mRNA.
DR   EMBL; AY072622; AAL62013.1; -; mRNA.
DR   EMBL; AY088308; AAM65847.1; -; mRNA.
DR   IPI; IPI00539763; -.
DR   PIR; S52380; S52380.
DR   RefSeq; NP_178022.1; -.
DR   UniGene; At.24660; -.
DR   HSSP; P00198; 2FDN.
DR   PRIDE; Q42599; -.
DR   GeneID; 844242; -.
DR   GenomeReviews; CT485782_GR; AT1G79010.
DR   KEGG; ath:AT1G79010; -.
DR   NMPDR; fig|3702.1.peg.7463; -.
DR   GeneFarm; 1821; 140.
DR   TAIR; At1g79010; -.
DR   OMA; Q42599; EMVRGLM.
DR   BioCyc; MetaCyc:AT1G79010-MON; -.
DR   BRENDA; 1.6.5.3; 302.
DR   BRENDA; 1.6.99.3; 302.
DR   ArrayExpress; Q42599; -.
DR   GermOnline; AT1G79010; Arabidopsis thaliana.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0045271; C:respiratory chain complex I; IDA:TAIR.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR001450; 4Fe4S_Fe_S_bd_subgr.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR   Pfam; PF00037; Fer4; 2.
DR   TIGRFAMs; TIGR01971; NuoI; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Mitochondrion; NAD; Oxidoreductase; Repeat;
KW   Respiratory chain; Transit peptide; Transport; Ubiquinone.
FT   TRANSIT       1      ?       Mitochondrion (By similarity).
FT   CHAIN         ?    222       NADH dehydrogenase [ubiquinone] iron-
FT                                sulfur protein 8, mitochondrial.
FT                                /FTId=PRO_0000020016.
FT   DOMAIN      114    143       4Fe-4S ferredoxin-type 1.
FT   DOMAIN      153    182       4Fe-4S ferredoxin-type 2.
FT   METAL       123    123       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       126    126       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       129    129       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       133    133       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       162    162       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       165    165       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       168    168       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       172    172       Iron-sulfur 1 (4Fe-4S) (By similarity).
SQ   SEQUENCE   222 AA;  25503 MW;  7C1F2264B0D0631B CRC64;
     MASILARRSL NTLRARHLVL SGQALQGSHL SRLQSRGISY GSNKDDEEAE QLSKEISKDW
     NTVFERSINT LFLTEMVRGL SLTLKYFFDP KVTINYPFEK GPLSPRFRGE HALRRYPTGE
     ERCIACKLCE AVCPAQAITI EAEEREDGSR RTTRYDIDMT KCIYCGFCQE ACPVDAIVEG
     PNFEFATETH EELLYDKEKL LENGDRWETE IAENLRSESL YR
//