ID A0A505DR50_9ACTN Unreviewed; 834 AA.
AC A0A505DR50;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN ORFNames=FGD71_002240 {ECO:0000313|EMBL:TPQ23788.1};
OS Streptomyces sporangiiformans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2315329 {ECO:0000313|EMBL:TPQ23788.1, ECO:0000313|Proteomes:UP000317378};
RN [1] {ECO:0000313|EMBL:TPQ23788.1, ECO:0000313|Proteomes:UP000317378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-SSA 1 {ECO:0000313|EMBL:TPQ23788.1,
RC ECO:0000313|Proteomes:UP000317378};
RA Han L.;
RT "Streptomyces sporangiiformans sp. nov., a novel actinomycete isolated from
RT soil in Mount Song.";
RL Submitted (JUN-2019) 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 -!- 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:TPQ23788.1}.
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DR EMBL; VCHX02000037; TPQ23788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A505DR50; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000317378; 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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
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; 2.20.25.90; ADC-like domains; 1.
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; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
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:SF12; NADH-QUINONE OXIDOREDUCTASE SUBUNIT G; 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; PF01568; Molydop_binding; 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}; NAD {ECO:0000256|RuleBase:RU003525};
KW Oxidoreductase {ECO:0000313|EMBL:TPQ23788.1};
KW Quinone {ECO:0000256|RuleBase:RU003525};
KW Reference proteome {ECO:0000313|Proteomes:UP000317378};
KW Translocase {ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 20..98
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 100..139
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 238..294
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 834 AA; 87815 MW; E847871A9B3AAA27 CRC64;
MTVTTSAPSG GGEAAVPPED LVTLTIDGIE ISVPKGTLVI RAAEQLGIEI PRFCDHPLLA
PAGACRQCIV EVEGQRKPMA SCTITCTDGM VVKTHLTSPV AEKAQKGVME LLLINHPLDC
PVCDKGGECP LQNQAMSHGH AESRFEGKKR TFEKPVPISA QVLLDRERCV LCARCTRFSN
QVAGDPMIEL LERGALQQVG TGEGDPFESY FSGNTIQICP VGALTSSAYR FRSRPFDLVS
SPSVCEHCSG GCATRTDHRR GKVMRRLAAN DPEVNEEWMC DKGRFGFRYA QQRDRLTTPL
VRGASGELEP ASWPEALAAA AEGLTAARSR TGVLTGGRLT VEDAYAYSKF ARVALDTNDI
DFRARVHSSE EADFLAARVA GRGRDLDGTG VTYTSLEKAP AVLLVGIESE EEAPGVFLRL
RKAWRGHGQQ TFSLATHATR GLEKAGGTLL PAAPGTETEW LDALASGVGL DGQGATASEA
LRAEGAVIVV GERLAAVAGG LTAVARAATA TGAHLVWIPR RAGERGAIEA GALPSLLPGG
RPATDPRARD EVAAAWGVAE LPHRYGRDTG QIVEAAATGE LSALVVAGVE IADLPDPARA
REALSEVGFL VSFELRPSEV TEHADVVLPV AAVVEKAGTF LNWEGRARLF EAALKPDQMS
RRLPPTDARV LQMLADAMDV HLGLPDLRTA RVELDRLGAW DGARATEPME SAAQLPRPAA
GEAVLAGHRL LLDQGRLQEG DEALAATRHA AHARVSAATA AEAGVKNGDA LAVTGPSGVV
ELPLQITEMP DRVVWLPLNS AGGGVASDTG AQPGALVRIG PATLATEAPK EVEA
//
