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Database: UniProt
Entry: A0A1F5ABC4_9BACT
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ID   A0A1F5ABC4_9BACT        Unreviewed;       528 AA.
AC   A0A1F5ABC4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=NADP oxidoreductase {ECO:0000313|EMBL:OGD15829.1};
GN   ORFNames=A2V47_01455 {ECO:0000313|EMBL:OGD15829.1};
OS   Candidatus Atribacteria bacterium RBG_19FT_COMBO_35_14.
OC   Bacteria; Atribacterota.
OX   NCBI_TaxID=1797291 {ECO:0000313|EMBL:OGD15829.1, ECO:0000313|Proteomes:UP000177701};
RN   [1] {ECO:0000313|EMBL:OGD15829.1, ECO:0000313|Proteomes:UP000177701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGD15829.1}.
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DR   EMBL; MEYH01000047; OGD15829.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5ABC4; -.
DR   STRING; 1797291.A2V47_01455; -.
DR   Proteomes; UP000177701; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   CDD; cd02980; TRX_Fd_family; 1.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 6.10.250.1450; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
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   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   PANTHER; PTHR43578:SF1; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 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.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 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   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          440..485
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
SQ   SEQUENCE   528 AA;  57750 MW;  3D49EE4608FD367F CRC64;
     MSKRSIAQVL VGIDGNTVLF GARKIKTKLI TEMHKHGLSE QVQVIETGSI GPANQGVIIG
     VYPAGEMYGN ITEEEVVEFV QERFVKGRPY KKLLLSEKLP AGIDLTAYDS RKTQYLGRIV
     LDNCGKINPE DIEEYIGMRG YEALGIILKE KTSEEVIKIV RDSGLKGRGG AGFPTGLKWS
     FTAKVKDTPK YVICNADEGE PGTFKDRLIM EGDPHKVLEG MAICGYAIGA NTGYIYIRGE
     YQLSIQRLEK AIKDAEKLGL LGENIFGTDF DFQVKIKIGA GSYVCGEETA LLTSMEGFRG
     EPRFKPPFPA ESGFLAKPTN INNVETFANI APIILNGAEW FKKLGTESSS GTKVYTVLGH
     IKRSGLIEVP MGVTLREIIY DYAGGMSSGN FKMTQIGGTA GNLLSSEFLD VPLDFQSLKE
     VGYSLGSGAV LIMNETVSVV DFIKCCMKFF VHESCGKCTP CREGTRYAYE ILDKISLGKG
     KADDIESLKL LGESMKDSSF CPFGQSAPNS LLNSLSLFPE EYNNLLIK
//
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