NDUS1_MOUSE
ID NDUS1_MOUSE Reviewed; 727 AA.
AC Q91VD9; Q3UQ73; Q8BM16;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;
DE EC=7.1.1.2 {ECO:0000269|PubMed:27799543, ECO:0000269|PubMed:32072193};
DE AltName: Full=Complex I-75kD;
DE Short=CI-75kD;
DE Flags: Precursor;
GN Name=Ndufs1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic breast, Heart, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 77-84; 88-108; 185-212; 247-266; 277-289; 292-299;
RP 312-325; 361-382; 409-417; 421-441; 451-467; 471-483; 502-511; 519-539;
RP 544-557; 608-617; 625-643; 646-655; 674-702 AND 713-727, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-467; LYS-499 AND LYS-709,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [8]
RP FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=27799543; DOI=10.1073/pnas.1613701113;
RA Lopez-Fabuel I., Le Douce J., Logan A., James A.M., Bonvento G.,
RA Murphy M.P., Almeida A., Bolanos J.P.;
RT "Complex I assembly into supercomplexes determines differential
RT mitochondrial ROS production in neurons and astrocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:13063-13068(2016).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP AKAP1.
RX PubMed=32072193; DOI=10.1007/s00125-020-05103-w;
RA Qi B., He L., Zhao Y., Zhang L., He Y., Li J., Li C., Zhang B., Huang Q.,
RA Xing J., Li F., Li Y., Ji L.;
RT "Akap1 deficiency exacerbates diabetic cardiomyopathy in mice by NDUFS1-
RT mediated mitochondrial dysfunction and apoptosis.";
RL Diabetologia 63:1072-1087(2020).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC NADH through the respiratory chain, using ubiquinone as an electron
CC acceptor (PubMed:27799543, PubMed:32072193). Essential for catalysing
CC the entry and efficient transfer of electrons within complex I
CC (PubMed:27799543). Plays a key role in the assembly and stability of
CC complex I and participates in the association of complex I with
CC ubiquinol-cytochrome reductase complex (Complex III) to form
CC supercomplexes (PubMed:27799543). {ECO:0000269|PubMed:27799543,
CC ECO:0000269|PubMed:32072193}.
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 Evidence={ECO:0000269|PubMed:27799543, ECO:0000269|PubMed:32072193};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:Q56223};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000250|UniProtKB:Q56223};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q56223};
CC Note=Binds 2 [4Fe-4S] clusters per subunit.
CC {ECO:0000250|UniProtKB:Q56223};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits (By similarity). This is
CC the largest subunit of complex I and it is a component of the iron-
CC sulfur (IP) fragment of the enzyme (By similarity). Complex I
CC associates with ubiquinol-cytochrome reductase complex (Complex III) to
CC form supercomplexes (PubMed:27799543). In astrocytes, less complex I is
CC assembled into supercomplexes as compared to neurons (PubMed:27799543).
CC Interacts with MDM2 (By similarity). Interacts with AKAP1
CC (PubMed:32072193). {ECO:0000250|UniProtKB:P15690,
CC ECO:0000250|UniProtKB:P28331, ECO:0000269|PubMed:27799543,
CC ECO:0000269|PubMed:32072193}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P15690}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P15690}; Matrix side
CC {ECO:0000250|UniProtKB:P15690}.
CC -!- TISSUE SPECIFICITY: Brain. More abundant in neurons than in astrocytes
CC (at protein level). {ECO:0000269|PubMed:27799543}.
CC -!- PTM: Acetylation of Lys-84 is observed in liver mitochondria from
CC fasted mice but not from fed mice.
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AK034597; BAE20494.1; -; mRNA.
DR EMBL; AK036926; BAC29641.1; -; mRNA.
DR EMBL; AK142711; BAE25170.1; -; mRNA.
DR EMBL; AL645950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466548; EDL00180.1; -; Genomic_DNA.
DR EMBL; CH466548; EDL00181.1; -; Genomic_DNA.
DR EMBL; CH466548; EDL00182.1; -; Genomic_DNA.
DR EMBL; CH466548; EDL00184.1; -; Genomic_DNA.
DR EMBL; BC006660; AAH06660.1; -; mRNA.
DR EMBL; BC015300; AAH15300.1; -; mRNA.
DR CCDS; CCDS14996.1; -.
DR RefSeq; NP_001153510.1; NM_001160038.1.
DR RefSeq; NP_001153511.1; NM_001160039.1.
DR RefSeq; NP_001153512.1; NM_001160040.1.
DR RefSeq; NP_663493.2; NM_145518.2.
DR RefSeq; XP_006496015.1; XM_006495952.3.
DR PDB; 6G2J; EM; 3.30 A; G=1-727.
DR PDB; 6G72; EM; 3.90 A; G=1-727.
DR PDB; 6ZR2; EM; 3.10 A; G=1-727.
DR PDB; 6ZTQ; EM; 3.00 A; G=1-727.
DR PDB; 7AK5; EM; 3.17 A; G=1-715.
DR PDB; 7AK6; EM; 3.82 A; G=1-727.
DR PDB; 7B93; EM; 3.04 A; G=1-727.
DR PDB; 7PSA; EM; 3.40 A; G=1-727.
DR PDBsum; 6G2J; -.
DR PDBsum; 6G72; -.
DR PDBsum; 6ZR2; -.
DR PDBsum; 6ZTQ; -.
DR PDBsum; 7AK5; -.
DR PDBsum; 7AK6; -.
DR PDBsum; 7B93; -.
DR PDBsum; 7PSA; -.
DR AlphaFoldDB; Q91VD9; -.
DR SMR; Q91VD9; -.
DR BioGRID; 230599; 78.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; Q91VD9; -.
DR IntAct; Q91VD9; 9.
DR MINT; Q91VD9; -.
DR STRING; 10090.ENSMUSP00000027111; -.
DR iPTMnet; Q91VD9; -.
DR PhosphoSitePlus; Q91VD9; -.
DR SwissPalm; Q91VD9; -.
DR REPRODUCTION-2DPAGE; IPI00308882; -.
DR REPRODUCTION-2DPAGE; Q91VD9; -.
DR EPD; Q91VD9; -.
DR jPOST; Q91VD9; -.
DR MaxQB; Q91VD9; -.
DR PaxDb; Q91VD9; -.
DR PeptideAtlas; Q91VD9; -.
DR PRIDE; Q91VD9; -.
DR ProteomicsDB; 252872; -.
DR Antibodypedia; 34175; 317 antibodies from 37 providers.
DR DNASU; 227197; -.
DR Ensembl; ENSMUST00000027111; ENSMUSP00000027111; ENSMUSG00000025968.
DR Ensembl; ENSMUST00000168099; ENSMUSP00000126621; ENSMUSG00000025968.
DR GeneID; 227197; -.
DR KEGG; mmu:227197; -.
DR UCSC; uc007bfu.2; mouse.
DR CTD; 4719; -.
DR MGI; MGI:2443241; Ndufs1.
DR VEuPathDB; HostDB:ENSMUSG00000025968; -.
DR eggNOG; KOG2282; Eukaryota.
DR GeneTree; ENSGT00940000153514; -.
DR HOGENOM; CLU_000422_11_6_1; -.
DR InParanoid; Q91VD9; -.
DR OMA; HKNVGPL; -.
DR OrthoDB; 1095510at2759; -.
DR PhylomeDB; Q91VD9; -.
DR TreeFam; TF105756; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 227197; 24 hits in 73 CRISPR screens.
DR ChiTaRS; Ndufs1; mouse.
DR PRO; PR:Q91VD9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91VD9; protein.
DR Bgee; ENSMUSG00000025968; Expressed in myocardium of ventricle and 288 other tissues.
DR ExpressionAtlas; Q91VD9; baseline and differential.
DR Genevisible; Q91VD9; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; ISS:UniProtKB.
DR GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB.
DR GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISO:MGI.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR CDD; cd00207; fer2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR InterPro; IPR015405; NuoG_C.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR Pfam; PF09326; NADH_dhqG_C; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR01973; NuoG; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; 4Fe-4S; Acetylation; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Respiratory chain; Transit peptide;
KW Translocase; Transport; Ubiquinone.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P15690"
FT CHAIN 24..727
FT /note="NADH-ubiquinone oxidoreductase 75 kDa subunit,
FT mitochondrial"
FT /id="PRO_0000019969"
FT DOMAIN 30..108
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 108..147
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT DOMAIN 245..301
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 64
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:Q56223"
FT BINDING 75
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:Q56223"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:Q56223"
FT BINDING 92
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:Q56223"
FT BINDING 124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 131
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 137
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 176
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q56223"
FT BINDING 179
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q56223"
FT BINDING 182
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q56223"
FT BINDING 226
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q56223"
FT MOD_RES 84
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 467
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 499
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 709
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 491
FT /note="V -> A (in Ref. 4; AAH06660/AAH15300)"
FT /evidence="ECO:0000305"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 107..122
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:7B93"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:7AK5"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 235..239
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:7B93"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 319..332
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:6ZR2"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 349..359
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:7B93"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 391..396
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 398..404
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 412..424
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:6ZR2"
FT HELIX 450..457
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 461..466
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 470..477
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 478..482
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:7AK5"
FT HELIX 486..503
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:7AK5"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 520..522
FT /evidence="ECO:0007829|PDB:6ZR2"
FT HELIX 523..528
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:7AK5"
FT HELIX 535..539
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 552..555
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:7B93"
FT STRAND 565..572
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 574..577
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 581..585
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 619..629
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 639..649
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 665..672
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 691..693
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 700..702
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 705..714
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 727 AA; 79777 MW; 4A4B4BD6C330BB4F CRC64;
MLRIPIKRAL IGLSNSPKGY VRTTGTAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI
PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSEKSK KAREGVMEFL
LANHPLDCPI CDQGGECDLQ DQSMMFGSDR SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT
RCIRFASEIA GVDDLGTTGR GNDMQVGTYI EKMFMSELSG NVIDICPVGA LTSKPYAFTA
RPWETRKTES IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ
RLTEPMVRNE KGLLTYTSWE DALSRVAGML QNFEGNAVAA IAGGLVDAEA LVALKDLLNK
VDSDNLCTEE IFPTEGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK
SWLHNDLKVA LIGSPVDLTY RYDHLGDSPK ILQDIASGRH SFCEVLKDAK KPMVVLGSSA
LQRDDGAAIL VAVSNMVQKI RVTTGVAAEW KVMNILHRIA SQVAALDLGY KPGVEAIRKN
PPKMLFLLGA DGGCITRQDL PKDCFIVYQG HHGDVGAPMA DVILPGAAYT EKSATYVNTE
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GITLPYDTLD QVRNRLEEVS PNLVRYDDIE
ETNYFQQASE LAKLVNQEVL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA
VEEPSIC
