ID A0A3D9DCS1_9FLAO Unreviewed; 185 AA. AC A0A3D9DCS1; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 02-DEC-2020, entry version 7. 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; Weeksellaceae; OC 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., Park K.H., RA Kim S.B.; RT "Four new species of Chryseobacterium from the rhizosphere of coastal sand RT dune plants, Chryseobacterium elymi sp. nov., Chryseobacterium hagamense RT sp. nov., Chryseobacterium lathyri sp. nov. and Chryseobacterium RT rhizosphaerae sp. nov."; RL Syst. Appl. Microbiol. 33:122-127(2010). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur CC (Fe-S) centers, to quinones in the respiratory chain. The immediate CC electron acceptor for the enzyme in this species is believed to be CC ubiquinone. Couples the redox reaction to proton translocation (for CC every two electrons transferred, four hydrogen ions are translocated CC across the cytoplasmic membrane), and thus conserves the redox energy CC in a proton gradient. {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, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; CC 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 NuoA, H, CC J, K, L, M, N constitute the membrane sector of the complex. CC {ECO:0000256|HAMAP-Rule:MF_01351}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01351}; CC Peripheral membrane protein {ECO:0000256|HAMAP-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 EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01351}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01351}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01351}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_01351}; Membrane {ECO:0000256|HAMAP-Rule:MF_01351}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01351}; 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 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT DOMAIN 115..144 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT COILED 163..183 FT /evidence="ECO:0000256|SAM:Coils" FT METAL 78 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 81 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 84 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 88 FT /note="Iron-sulfur 2 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 124 FT /note="Iron-sulfur 2 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 127 FT /note="Iron-sulfur 2 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 130 FT /note="Iron-sulfur 2 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 134 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="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 //