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Database: UniProt
Entry: A0A0Q9AQ82_9ACTN
LinkDB: A0A0Q9AQ82_9ACTN
Original site: A0A0Q9AQ82_9ACTN 
ID   A0A0Q9AQ82_9ACTN        Unreviewed;       453 AA.
AC   A0A0Q9AQ82;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 51kDa subunit iron-sulphur binding domain-containing protein {ECO:0000259|SMART:SM00928};
GN   ORFNames=ASE41_03475 {ECO:0000313|EMBL:KRD19476.1};
OS   Streptomyces sp. Root264.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1736503 {ECO:0000313|EMBL:KRD19476.1, ECO:0000313|Proteomes:UP000051177};
RN   [1] {ECO:0000313|EMBL:KRD19476.1, ECO:0000313|Proteomes:UP000051177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root264 {ECO:0000313|EMBL:KRD19476.1,
RC   ECO:0000313|Proteomes:UP000051177};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRD19476.1, ECO:0000313|Proteomes:UP000051177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root264 {ECO:0000313|EMBL:KRD19476.1,
RC   ECO:0000313|Proteomes:UP000051177};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00007523}.
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:KRD19476.1}.
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DR   EMBL; LMIZ01000012; KRD19476.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q9AQ82; -.
DR   STRING; 1736503.ASE41_03475; -.
DR   Proteomes; UP000051177; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR   Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR   InterPro; IPR011538; Nuo51_FMN-bd.
DR   InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR   InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR   InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR   InterPro; IPR019554; Soluble_ligand-bd.
DR   PANTHER; PTHR11780:SF10; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11780; NADH-UBIQUINONE OXIDOREDUCTASE FLAVOPROTEIN 1 NDUFV1; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   Pfam; PF10531; SLBB; 1.
DR   SMART; SM00928; NADH_4Fe-4S; 1.
DR   SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR   SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR   SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051177};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          341..385
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   453 AA;  47468 MW;  4DA2DF7088C33160 CRC64;
     MNSSALTPNS SAVTQHTTRR PSPVRHDAAL RLLAAWHATG RAATLADHLE RHGPSPVAAV
     LTAHGSAALV EAAETAGLTG RGGAGFPTAR KLRAVAERRG RAVVVVNAME SEPASGKDRF
     LLTVAPHLVL DGAVLAAAAI GADTVHVCLP RDRSTRHEQL DAAVEERRRA RVDPVRLRLH
     TLPHAYVSSE STSLVRWLNG GPARPEGGPP RPHERGVDRR PTLVHNVETL AHLALVARYG
     SDWFRQAGTP DEPGTTLVTV SGAVAAPGVR EVALGTPLTT VLDRAGGPTE RLDAVLLGGF
     AGTWLPEAHL HTPLARRDLA PLGAAPGAGV LIALPRSACG LTETARMLAY LAAHSARQCG
     PCRLGLPAVA GDFTALAAGR ADADLLSRLH RRTGLLPDRG ACRHPDGAAR LAASALRAFS
     DDVGRHLADG ACPEARQPPR IPVPSAEPPQ TWR
//
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