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 27-MAR-2024, entry version 185. 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, RC Pancreas, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8OLT; EM; 2.84 A; G=1-727. DR PDB; 8OM1; EM; 2.39 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 PDBsum; 8OLT; -. DR PDBsum; 8OM1; -. DR AlphaFoldDB; Q91VD9; -. DR EMDB; EMD-11377; -. DR EMDB; EMD-11424; -. DR EMDB; EMD-11810; -. DR EMDB; EMD-11811; -. DR EMDB; EMD-12095; -. DR EMDB; EMD-13611; -. DR EMDB; EMD-16962; -. DR EMDB; EMD-16965; -. DR EMDB; EMD-4345; -. DR EMDB; EMD-4356; -. DR SMR; Q91VD9; -. DR BioGRID; 230599; 82. DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I. DR CORUM; Q91VD9; -. DR IntAct; Q91VD9; 9. DR MINT; Q91VD9; -. DR STRING; 10090.ENSMUSP00000027111; -. DR GlyGen; Q91VD9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q91VD9; -. DR MetOSite; 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; 10090-ENSMUSP00000027111; -. DR PeptideAtlas; Q91VD9; -. DR ProteomicsDB; 252872; -. DR Pumba; Q91VD9; -. DR Antibodypedia; 34175; 354 antibodies from 37 providers. DR DNASU; 227197; -. DR Ensembl; ENSMUST00000027111.15; ENSMUSP00000027111.9; ENSMUSG00000025968.17. DR Ensembl; ENSMUST00000168099.9; ENSMUSP00000126621.3; ENSMUSG00000025968.17. DR GeneID; 227197; -. DR KEGG; mmu:227197; -. DR UCSC; uc007bfu.2; mouse. DR AGR; MGI:2443241; -. 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; QDQAMAY; -. DR OrthoDB; 19999at2759; -. 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; 25 hits in 77 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 292 other cell types or tissues. DR ExpressionAtlas; Q91VD9; baseline and differential. 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; IEA:UniProtKB-KW. 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; NAS: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; NAS: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 CDD; cd02773; MopB_Res-Cmplx1_Nad11; 1. DR Gene3D; 3.10.20.740; -; 1. DR Gene3D; 3.30.200.210; -; 1. DR Gene3D; 3.30.70.20; -; 1. DR Gene3D; 3.40.50.740; -; 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; NDUFS1-like_C. DR NCBIfam; TIGR01973; NuoG; 1. DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1. DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1. DR Pfam; PF13510; Fer2_4; 1. 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; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 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. DR Genevisible; Q91VD9; MM. 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:8OM1" FT STRAND 39..43 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 49..55 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:6ZTQ" FT STRAND 79..82 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 86..90 FT /evidence="ECO:0007829|PDB:6ZTQ" FT TURN 91..93 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 107..122 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 128..130 FT /evidence="ECO:0007829|PDB:8OM1" FT TURN 132..135 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 138..146 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 167..171 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 181..188 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 196..199 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:8OM1" FT TURN 217..220 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 221..225 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:7AK5" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:8OM1" FT TURN 234..238 FT /evidence="ECO:0007829|PDB:8OM1" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 246..251 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 254..257 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 260..266 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 269..275 FT /evidence="ECO:0007829|PDB:8OM1" FT TURN 279..282 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 288..292 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 293..298 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 299..301 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 306..308 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 319..332 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 338..342 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 348..360 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 365..370 FT /evidence="ECO:0007829|PDB:8OM1" FT TURN 376..379 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 382..385 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 386..389 FT /evidence="ECO:0007829|PDB:6ZTQ" FT HELIX 392..395 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 398..404 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 407..410 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 412..424 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 428..434 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 443..448 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 451..456 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 463..468 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 470..477 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 480..482 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 483..485 FT /evidence="ECO:0007829|PDB:7AK5" FT HELIX 486..504 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 508..510 FT /evidence="ECO:0007829|PDB:7AK5" FT STRAND 513..516 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 522..527 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 531..534 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 535..539 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 543..549 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 552..555 FT /evidence="ECO:0007829|PDB:6ZTQ" FT HELIX 557..559 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 565..572 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 574..576 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 577..579 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 581..586 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 589..591 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 595..597 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 603..605 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 619..629 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 639..649 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 651..654 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 665..673 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 691..693 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 699..702 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 705..713 FT /evidence="ECO:0007829|PDB:8OM1" 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 //