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Database: UniProt
Entry: A0A1J5HF04_9CYAN
LinkDB: A0A1J5HF04_9CYAN
Original site: A0A1J5HF04_9CYAN 
ID   A0A1J5HF04_9CYAN        Unreviewed;       246 AA.
AC   A0A1J5HF04;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit K {ECO:0000256|HAMAP-Rule:MF_01356};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01356};
DE   AltName: Full=NAD(P)H dehydrogenase I subunit K {ECO:0000256|HAMAP-Rule:MF_01356};
DE   AltName: Full=NDH-1 subunit K {ECO:0000256|HAMAP-Rule:MF_01356};
DE            Short=NDH-K {ECO:0000256|HAMAP-Rule:MF_01356};
GN   Name=ndhK {ECO:0000256|HAMAP-Rule:MF_01356};
GN   ORFNames=AUK48_03540 {ECO:0000313|EMBL:OIP77704.1};
OS   Oscillatoriales cyanobacterium CG2_30_44_21.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales.
OX   NCBI_TaxID=1805292 {ECO:0000313|EMBL:OIP77704.1, ECO:0000313|Proteomes:UP000185977};
RN   [1] {ECO:0000313|EMBL:OIP77704.1, ECO:0000313|Proteomes:UP000185977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG2_30_44_21 {ECO:0000313|EMBL:OIP77704.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
CC   -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via
CC       FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory
CC       and/or the photosynthetic chain. The immediate electron acceptor for
CC       the enzyme in this species is believed to be plastoquinone. Couples the
CC       redox reaction to proton translocation, and thus conserves the redox
CC       energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in
CC       inorganic carbon-concentration. {ECO:0000256|HAMAP-Rule:MF_01356}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC         H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01356};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC         H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01356};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01356};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_01356};
CC   -!- SUBUNIT: NDH-1 can be composed of about 15 different subunits;
CC       different subcomplexes with different compositions have been identified
CC       which probably have different functions. {ECO:0000256|HAMAP-
CC       Rule:MF_01356}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01356}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01356}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01356}.
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00009173, ECO:0000256|HAMAP-Rule:MF_01356,
CC       ECO:0000256|RuleBase:RU004464}.
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:OIP77704.1}.
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DR   EMBL; MNZA01000054; OIP77704.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5HF04; -.
DR   STRING; 1805292.AUK48_03540; -.
DR   Proteomes; UP000185977; Unassembled WGS sequence.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid 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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.12280; -; 1.
DR   HAMAP; MF_01356; NDH1_NuoB; 1.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR   NCBIfam; TIGR01957; nuoB_fam; 1.
DR   PANTHER; PTHR11995; NADH DEHYDROGENASE; 1.
DR   PANTHER; PTHR11995:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL; 1.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   SUPFAM; SSF56770; HydA/Nqo6-like; 1.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01356,
KW   ECO:0000256|RuleBase:RU004464}; Membrane {ECO:0000256|HAMAP-Rule:MF_01356};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01356,
KW   ECO:0000256|RuleBase:RU004464};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01356};
KW   Plastoquinone {ECO:0000256|ARBA:ARBA00022957, ECO:0000256|HAMAP-
KW   Rule:MF_01356};
KW   Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_01356};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01356};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01356};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01356}.
FT   DOMAIN          62..172
FT                   /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT                   /evidence="ECO:0000259|Pfam:PF01058"
FT   BINDING         62
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT   BINDING         63
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT   BINDING         127
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT   BINDING         158
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
SQ   SEQUENCE   246 AA;  27688 MW;  649DD38FEAE3E771 CRC64;
     MKPENISLDF SIEEQTQRLI NPAEKPQVTQ DLSNNVILTT LNDLYNWSRM SSLWPMLYGT
     SCCFIEFAAM IGSRFDFDRF GLLPRSSPRQ ADLLIVAGTV TMKMAPAMVR LYEQMQEPKY
     VIAMGACTIT GGMFSSDSYT TVRGVDKLVP VDVYIPGCPP RPEAIMDAII KLRKKIGTEG
     FQERANLNRT HRYYAVKHEM KVVSPILTGK YLEMPSRMAP PQELVESGIP LPALQMAQKE
     VETLGR
//
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