ID A0A269PLM8_9GAMM Unreviewed; 903 AA.
AC A0A269PLM8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN ORFNames=CJF42_17640 {ECO:0000313|EMBL:PAJ73125.1};
OS Pseudoalteromonas sp. NBT06-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=2025950 {ECO:0000313|EMBL:PAJ73125.1, ECO:0000313|Proteomes:UP000215836};
RN [1] {ECO:0000313|EMBL:PAJ73125.1, ECO:0000313|Proteomes:UP000215836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBT06-2 {ECO:0000313|EMBL:PAJ73125.1,
RC ECO:0000313|Proteomes:UP000215836};
RA Wei Y.;
RT "Pseudoalteromonas hadalis sp. nov., a facultative psychrophile isolated
RT from New Britain Trench.";
RL Submitted (AUG-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 -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F, and G
CC constitute the peripheral sector of the complex.
CC {ECO:0000256|ARBA:ARBA00026021}.
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:PAJ73125.1}.
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DR EMBL; NQMR01000100; PAJ73125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A269PLM8; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000215836; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000215836};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003525};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT DOMAIN 5..88
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 88..127
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 226..282
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 903 AA; 101885 MW; 8650EC288AD1DE4E CRC64;
MEMTNKVTLY IDNLSYQVPD NINLLQACLS LNMDVPYFCW HPALGSVGAC RQCAVMQYQN
EEDTRGRLVM SCMTPVTEGM RISFNNEKAH TFRATNIEAI MTNHPHDCPV CEEGGDCHLQ
DMTLLSGHIK RRYPGIKRTH NNQYLGPFLN HEMNRCIGCY RCVRFYRDYC GGKDLNVFSS
KNNIYFGRTE SGNLENEFSG NLAEVCPTGV FTDKPFSKHY IRKWDLQSSP SICTHCSIGC
NIYATERGGI IRKINNRLNQ DINGHFLCNR GRFGYQHVNH ENKISQVWSR DHQSNKTHAL
DNIHAHIKLK KWLNESNARI IGIGSPRSSI ENNAALHKLV GAHNFYAGIA KNELTQLNLL
TKTYESNQIN LLSLKEIEQT DTVLLVGEDV TQTAPRIALS IRQMTKNRGI NKAEKFGIKP
WQDEALRNIT QDTKSPLIII NTHESKLSDV AKQNLNLSPN KQLILLLEIE TYLVNNTSHC
SELAISIASD LLNANNPAII TGTHSFNIEL LSACLRISAI LKKQKNNSGF YCATSAVNTL
GLSLLCEPEQ DITHLIESIE SEPPTLLVIM ETDLFRYFSD KKLTTYLDKI KHIIVIDQLI
TDTVKMADLV LPATSFSEQN ATLINNEGRS QRAYAVMPAN DMRQTPYKWL AQHNSLDDDH
KLYQYIQSID SLLQPLSQFK SINKGDFTSA RQPLRSSART AFFANVDVKE YAPICDDKSN
LTYSMEGVSA FRQKTLDNTQ YKITTPVTGV WSPKWNSSQA INKTSLEDKN ESDLAVKIFN
TASAVPFEIP TAQQKTYNQP LNTISVCPHH HIYTNDDLAT FSSSIGELAP KPLIHMNQKQ
ANYLSIKSGE KLTITSNEYQ ISLPCEIHNT IADGVILVPF IEYIRLGTNI QVPSNYTDGE
YDD
//
