ID A0A3D9DCS1_9FLAO Unreviewed; 185 AA. AC A0A3D9DCS1; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 08-MAY-2019, entry version 3. DE RecName: Full=NADH-quinone oxidoreductase subunit I {ECO:0000256|HAMAP-Rule:MF_01351}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01351}; DE AltName: Full=NADH dehydrogenase I subunit I {ECO:0000256|HAMAP-Rule:MF_01351}; DE AltName: Full=NDH-1 subunit I {ECO:0000256|HAMAP-Rule:MF_01351}; GN Name=nuoI {ECO:0000256|HAMAP-Rule:MF_01351}; GN ORFNames=DRF60_14890 {ECO:0000313|EMBL:REC75796.1}; OS Chryseobacterium elymi. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=395936 {ECO:0000313|EMBL:REC75796.1, ECO:0000313|Proteomes:UP000257030}; RN [1] {ECO:0000313|EMBL:REC75796.1, ECO:0000313|Proteomes:UP000257030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 22547 {ECO:0000313|EMBL:REC75796.1, RC ECO:0000313|Proteomes:UP000257030}; RX PubMed=20185262; DOI=10.1016/j.syapm.2009.12.004; RA Cho S.H., Lee K.S., Shin D.S., Han J.H., Park K.S., Lee C.H., RA Park K.H., Kim S.B.; RT "Four new species of Chryseobacterium from the rhizosphere of coastal RT sand dune plants, Chryseobacterium elymi sp. nov., Chryseobacterium RT hagamense sp. nov., Chryseobacterium lathyri sp. nov. and RT Chryseobacterium rhizosphaerae sp. nov."; RL Syst. Appl. Microbiol. 33:122-127(2010). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. CC {ECO:0000256|HAMAP-Rule:MF_01351}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:132124; Evidence={ECO:0000256|HAMAP-Rule:MF_01351}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01351}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01351}; CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits CC NuoA, H, J, K, L, M, N constitute the membrane sector of the CC complex. {ECO:0000256|HAMAP-Rule:MF_01351}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01351}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01351}. CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family. CC {ECO:0000256|HAMAP-Rule:MF_01351}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:REC75796.1}. 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; QNUH01000013; REC75796.1; -; Genomic_DNA. DR Proteomes; UP000257030; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR HAMAP; MF_01351; NDH1_NuoI; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI. DR PANTHER; PTHR10849; PTHR10849; 1. DR Pfam; PF12838; Fer4_7; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01351}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01351}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000257030}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01351}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01351}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01351}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01351}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01351}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01351}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01351}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01351}. FT DOMAIN 69 98 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 115 144 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT COILED 163 183 {ECO:0000256|SAM:Coils}. FT METAL 78 78 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_01351}. FT METAL 81 81 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_01351}. FT METAL 84 84 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_01351}. FT METAL 88 88 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_01351}. FT METAL 124 124 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_01351}. FT METAL 127 127 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_01351}. FT METAL 130 130 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_01351}. FT METAL 134 134 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_01351}. SQ SEQUENCE 185 AA; 21026 MW; 1131C3C064D723E9 CRC64; MKLTNRSKVV SKKEMTLAEK IYLPAIFTGM GITFKHAVRT VIKGAPAVYS YPEVQKPRTT IWRGQHVLKR DEEGRERCTA CGLCAVACPA EAITMTAAER TKEEKGLYRE EKYASVYEIN MLRCIFCGMC EEACPKSAIY LTDRLVDVET NRGSFIYGKD KLVEKINERI DITTRQSEKQ KNAVK //