ID A0A4X1VKC6_PIG Unreviewed; 463 AA. AC A0A4X1VKC6; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 27-NOV-2024, entry version 26. DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial {ECO:0000256|ARBA:ARBA00020178}; DE AltName: Full=Complex I-49kD {ECO:0000256|ARBA:ARBA00030505}; DE AltName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit {ECO:0000256|ARBA:ARBA00031562}; GN Name=NDUFS2 {ECO:0000313|Ensembl:ENSSSCP00070043947.1}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00070043947.1, ECO:0000313|Proteomes:UP000314985}; RN [1] {ECO:0000313|Ensembl:ENSSSCP00070043947.1, ECO:0000313|Proteomes:UP000314985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Hannum G.I., Koren S., Schroeder S.G., Chin S.C., Nonneman D.J., RA Becker S.A., Rosen B.D., Bickhart D.M., Putnam N.H., Green R.E., RA Tuggle C.K., Liu H., Rohrer G.A., Warr A., Hall R., Kim K., Hume D.A., RA Talbot R., Chow W., Howe K., Schwartz A.S., Watson M., Archibald A.L., RA Phillippy A.M., Smith T.P.L.; RT "USMARCv1.0."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:7VBP, ECO:0007829|PDB:7VWL} RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS) OF 34-73. RX PubMed=35145322; DOI=10.1038/s41594-022-00722-w; RA Gu J., Liu T., Guo R., Zhang L., Yang M.; RT "The coupling mechanism of mammalian mitochondrial complex I."; RL Nat. Struct. Mol. Biol. 29:172-182(2022). RN [3] {ECO:0000313|Ensembl:ENSSSCP00070043947.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2023) to UniProtKB. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|ARBA:ARBA00001966}; CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex CC I) which is composed of 45 different subunits. Component of the iron- CC sulfur (IP) fragment of the enzyme. Interacts with NDUFAF3. Interacts CC with NDUFAF7. Interacts with CERS2. {ECO:0000256|ARBA:ARBA00046697}. CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family. CC {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|RuleBase:RU003685}. 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 RefSeq; XP_005663224.1; XM_005663167.2. DR PDB; 7VBP; EM; 2.80 A; Q=34-73. DR PDB; 7VWL; EM; 2.70 A; Q=34-73. DR PDB; 7VYI; EM; 3.10 A; Q=34-73. DR AlphaFoldDB; A0A4X1VKC6; -. DR EMDB; EMD-31884; -. DR EMDB; EMD-32155; -. DR EMDB; EMD-32206; -. DR SMR; A0A4X1VKC6; -. DR Ensembl; ENSSSCT00070051938.1; ENSSSCP00070043947.1; ENSSSCG00070025949.1. DR GeneID; 100156075; -. DR CTD; 4720; -. DR OrthoDB; 191at2759; -. DR Proteomes; UP000314985; Chromosome 4. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR FunFam; 1.10.645.10:FF:000005; NADH-quinone oxidoreductase subunit D; 1. DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1. DR HAMAP; MF_01358; NDH1_NuoD; 1. DR InterPro; IPR001135; NADH_Q_OxRdtase_suD. DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS. DR InterPro; IPR022885; NDH1_su_D/H. DR InterPro; IPR029014; NiFe-Hase_large. DR NCBIfam; TIGR01962; NuoD; 1. DR PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1. DR PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1. DR Pfam; PF00346; Complex1_49kDa; 1. DR SUPFAM; SSF56762; HydB/Nqo4-like; 1. DR PROSITE; PS00535; COMPLEX1_49K; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:7VBP, ECO:0007829|PDB:7VWL}; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485}; KW Iron {ECO:0000256|ARBA:ARBA00022485}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022485}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003685}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003685}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003685}. FT DOMAIN 193..463 FT /note="NADH-quinone oxidoreductase subunit D" FT /evidence="ECO:0000259|Pfam:PF00346" SQ SEQUENCE 463 AA; 52486 MW; 3649090E7B2BA586 CRC64; MAALRALCSL RGVAAQVLRP GAGARLPIQP SRGARQWQPD VEWAEQFGGA VMYPTKETAH WKPPPWNDVD PPKDTLVSNL TLNFGPQHPA AHGVLRLVME LSGEMVRKCD PHIGLLHRGT EKLIEYKTYL QALPYFDRLD YVSMMCNEQA YSLAVEKLLN IQPPPRAQWI RVLFGEITRL LNHIMAVTTH ALDIGAMTPF FWMFEEREKM FEFYERVSGA RMHAAYIRPG GVHQDLPLGL LDDIYEFSKN FSFRIDELEE MLTNNRIWRN RTVDIGVVTA EDALNYGFSG VMLRGSGIQW DLRKTQPYDV YDQVEFDVPI GSRGDCYDRY LCRVEEMRQS LRIISQCLNK MPPGEIKVDD AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI EAPKGEFGVY LVSDGSSRPY RCKIKAPGFA HLAGLDKMSK GHMLADVVAI IGTQDIVFGE VDR //