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Database: UniProt
Entry: A0A1G7RQ17_CHIFI
LinkDB: A0A1G7RQ17_CHIFI
Original site: A0A1G7RQ17_CHIFI 
ID   A0A1G7RQ17_CHIFI        Unreviewed;       903 AA.
AC   A0A1G7RQ17;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN   ORFNames=SAMN04488121_103561 {ECO:0000313|EMBL:SDG12765.1};
OS   Chitinophaga filiformis (Myxococcus filiformis) (Flexibacter filiformis).
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=104663 {ECO:0000313|EMBL:SDG12765.1, ECO:0000313|Proteomes:UP000199045};
RN   [1] {ECO:0000313|EMBL:SDG12765.1, ECO:0000313|Proteomes:UP000199045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 527 {ECO:0000313|EMBL:SDG12765.1,
RC   ECO:0000313|Proteomes:UP000199045};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNBN01000003; SDG12765.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7RQ17; -.
DR   STRING; 104663.SAMN04488121_103561; -.
DR   OrthoDB; 9805142at2; -.
DR   Proteomes; UP000199045; 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   CDD; cd02788; MopB_CT_NDH-1_NuoG2-N7; 1.
DR   CDD; cd02771; MopB_NDH-1_NuoG2-N7; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.20.740; -; 1.
DR   Gene3D; 3.30.200.210; -; 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; IPR009010; Asp_de-COase-like_dom_sf.
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   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; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 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; SSF50692; ADC-like; 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.
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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003525};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003525};
KW   Quinone {ECO:0000256|RuleBase:RU003525};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003525}.
FT   DOMAIN          1..83
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          83..122
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          221..277
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   903 AA;  99791 MW;  B912996CE561016B CRC64;
     MPTIYIDNKP FDVKAGKNLL EACLSLGIDL PYFCWHPAMG SVGACRQCAI KVFKDEEDTR
     GRLVMSCMEG VKDGMRISVE DETAKTFRSQ VVAWLMTNHP HDCPVCDEGG CCHLQDMTVM
     SGHNYRHYHF KKRTYPNQYL GPLINHEMNR CIQCYRCVRF YHDYAGGKDL NVFAAHNHVY
     FGREKDGVLE SPFSGNLVEV CPTGVFTDKT LKEHYTRKWD LTNAPSVCQH CSLGCNTIAG
     ERYGQLRNVV NRYNHEVNGY FLCDKGRFGY EFVNSENRIT QPLIRNQAIE AAGHDTVLQY
     MRTLVSGHTL IGIGSPRASL ESNYALMELV GKENFYQGVP DDLVYVEQKI VDILQAGCIH
     TPSLHEIEQA DAVLVLGEDI WNTAPIMALA VRQSVMKTAA THTTEQLPIP TWHDAAIKEL
     VQDDKGFLAN VTMLPSPLDE ISSATMKAAP DDMARLGFAI AHILNPSLPE VPHAGEELLA
     KAADISKALQ EAKHPVIIAG TSCWNNALIR AAFDIAAALH INEKKAGLAF VMQDCNSMGL
     AMMRASSFDR AVANIQRAAN NVTAIILEND LYRSIPAAKV DAFFSKCKHI VVLDTLHNRT
     TEKAHVLIPA ATFAEADGTF VNNEARAQRS SQVFMPANSE IRESFKWLAD VKALLNTVSN
     GHAKHMEDLL VALENKYPQF AGVSRVAPPH DFRIHGARIP RESHRYSGRT AMLANMTVSE
     PKPLQDDDSS LSYTMEGYRG LPPSPLIPFF WAPGWNSGQS VTKYQEEAGG ALKGGDPGVR
     LFEQTTTPPV FSKDIPDAFT PRVGKWMLLP QYHLFGSGEL SVYTKGIASQ SPEPYVSLSK
     RDAEQAQLKN GDTVSVKSDG KTYALPLSIN ESLPDGIMLV PAGLTGMEAL SWGAWINHST
     VTV
//
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