GenomeNet

Database: UniProt
Entry: A0A239JCK1_9SPHN
LinkDB: A0A239JCK1_9SPHN
Original site: A0A239JCK1_9SPHN 
ID   A0A239JCK1_9SPHN        Unreviewed;       667 AA.
AC   A0A239JCK1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN   ORFNames=SAMN06295912_13312 {ECO:0000313|EMBL:SNT03567.1};
OS   Sphingomonas laterariae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=861865 {ECO:0000313|EMBL:SNT03567.1, ECO:0000313|Proteomes:UP000198281};
RN   [1] {ECO:0000313|Proteomes:UP000198281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LNB2 {ECO:0000313|Proteomes:UP000198281};
RA   Varghese N., Submissions S.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC       reaction to proton translocation (for every two electrons transferred,
CC       four hydrogen ions are translocated across the cytoplasmic membrane),
CC       and thus conserves the redox energy in a proton gradient.
CC       {ECO:0000256|RuleBase:RU003525}.
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|ARBA:ARBA00000100,
CC         ECO:0000256|RuleBase:RU003525};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|RuleBase:RU003525};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000256|RuleBase:RU003525};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         ECO:0000256|RuleBase:RU003525};
CC   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00005404, ECO:0000256|RuleBase:RU003525}.
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; FZOS01000033; SNT03567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239JCK1; -.
DR   OrthoDB; 9816402at2; -.
DR   Proteomes; UP000198281; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.740; -; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|RuleBase:RU003525};
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU003525};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003525};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU003525};
KW   Metal-binding {ECO:0000256|RuleBase:RU003525};
KW   NAD {ECO:0000256|RuleBase:RU003525};
KW   Quinone {ECO:0000256|RuleBase:RU003525};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198281};
KW   Translocase {ECO:0000256|RuleBase:RU003525}.
FT   DOMAIN          2..79
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          79..118
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          216..272
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   667 AA;  71473 MW;  92AD8D23BD4C4BB3 CRC64;
     MPKLTVDGIE VEVPAGATVL QACEAAGKEI PRFCYHERLS IAGNCRMCLV EVKPGPPKPQ
     ASCALPAADN QEVRTDSLLV KKAREGVMEF LLINHPLDCP ICDQGGECDL QDQSVAYGRG
     NSRYDENKRA VTEKYMGPIV KTVMTRCIQC TRCVRFAEEV AGVEEIGAIY RGENMQITSY
     LEKAVSSELS GNVVDLCPVG ALTSKPYAFE ARPWELKKTA GIDVMDAVGT NIRIDARGRQ
     VLRVLPRIND DVNEEWASDK TRHAVDGLIR RRLDKPFLRK DGKLVPVTWG EAFQAIANVK
     AGASVAAIAG DMLDCETMYA AKKLLGAMGS DLLEGRQTGL DYDCTNLAAV NFNSTIAGIE
     TADAILIVGS NVRWEAPLVN TRIRKAVKAG AQVFVVGPEI DLTYKATWLG NDLSLLGNLP
     QEVKDAFTAA QRPALILGGG GLKAGAHGAT LALVGPLGLI KENWNGYNVL HMAASRMGGL
     MLGYAQPGGI GAVAAKQPKL VFLLGADEVA EDRFAKSFKV YVGHHGDRGA AQADVILPAA
     AYTEKAGTYV NLEGRVQRSD RAVFAPGDAR EDWAILRALS DVLGHTLPFD TFDALRAAMV
     ADVPALGELG LATYDWAPPA LDAAASGEIG YPIADFYLTN PIARASETMQ RCSAELIHGE
     SFAEAAE
//
DBGET integrated database retrieval system