(data stored in ACNUC1104 zone)

SWISSPROT: A1SE32_NOCSJ

ID   A1SE32_NOCSJ            Unreviewed;       440 AA.
AC   A1SE32;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000256|RuleBase:RU364066};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU364066};
GN   OrderedLocusNames=Noca_0525 {ECO:0000313|EMBL:ABL80067.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL80067.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL80067.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C.,
RA   Copeland A., Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A.,
RA   Hammon N.M., Han S., Hauser L.J., Israni S., Kim E., Kyrpides N.,
RA   Land M.L., Lapidus A., Larimer F.W., Lucas S., Pitluck S.,
RA   Richardson P., Schmutz J., Tapia R., Thompson S., Tice H.N.,
RA   Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing
RT   actinomycete Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC       sulfur (Fe-S) centers, to quinones in the respiratory chain.
CC       {ECO:0000256|RuleBase:RU364066}.
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,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132124; Evidence={ECO:0000256|RuleBase:RU364066};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|RuleBase:RU364066};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU364066,
CC         ECO:0000256|SAAS:SAAS00943848};
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|RuleBase:RU364066}.
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DR   EMBL; CP000509; ABL80067.1; -; Genomic_DNA.
DR   STRING; 196162.Noca_0525; -.
DR   EnsemblBacteria; ABL80067; ABL80067; Noca_0525.
DR   KEGG; nca:Noca_0525; -.
DR   eggNOG; ENOG4107QIZ; Bacteria.
DR   eggNOG; COG1894; LUCA.
DR   HOGENOM; HOG000251534; -.
DR   KO; K00335; -.
DR   OMA; CTMDYDS; -.
DR   BioCyc; NSP196162:GH4V-529-MONOMER; -.
DR   Proteomes; UP000000640; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD 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   Gene3D; 1.20.1440.230; -; 1.
DR   Gene3D; 3.40.50.11540; -; 1.
DR   InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR   InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
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   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; SSF140490; SSF140490; 1.
DR   SUPFAM; SSF142019; SSF142019; 1.
DR   TIGRFAMs; TIGR01959; nuoF_fam; 1.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1SE32.
DR   SWISS-2DPAGE; A1SE32.
KW   4Fe-4S {ECO:0000256|RuleBase:RU364066, ECO:0000256|SAAS:SAAS00943857};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000640};
KW   Flavoprotein {ECO:0000256|RuleBase:RU364066};
KW   FMN {ECO:0000256|RuleBase:RU364066};
KW   Iron {ECO:0000256|RuleBase:RU364066, ECO:0000256|SAAS:SAAS00943838};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU364066,
KW   ECO:0000256|SAAS:SAAS00943845};
KW   Metal-binding {ECO:0000256|RuleBase:RU364066,
KW   ECO:0000256|SAAS:SAAS00943864}; NAD {ECO:0000256|RuleBase:RU364066};
KW   Oxidoreductase {ECO:0000313|EMBL:ABL80067.1};
KW   Quinone {ECO:0000256|RuleBase:RU364066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640}.
FT   DOMAIN      332    377       NADH_4Fe-4S. {ECO:0000259|SMART:SM00928}.
SQ   SEQUENCE   440 AA;  47191 MW;  7CB569D4B8D8ADBC CRC64;
     MSDAVTDVLT PVLTDNWDQE RSWTLAAYES RGGYRAVDTA FAMEPDAVID AVKESGLRGR
     GGAGFPTGMK WGFIPQDNPR PKYLVVNADE SEPGTCKDIP LMMASPHTLV EGVIISSYAI
     RANKAFIYIR GEVLHVIRRV QRAVQEAYAA GHLGTNIHGS GFDLDVVVHA GAGAYICGEE
     TALLEGLEGR RGQPRLRPPF PAVAGLYASP TVINNVESIS SVPSIIGRGH AWFASMGTEK
     SKGVGIFSLS GHVKRPGQYE APLGITLRTL IDLAGGIREG HELKFWTPGG SSTPLLTAEH
     LDVPLDFEGV GSAGSMLGTR ALQIFDDSVC VVRAVLRWSE FYKHESCGKC TPCREGTWWL
     VQVLTALEKG DGTEEDLDLL LDQCDNILGR SFCALADGAT SPIVSSIQFF RDEYVAHLTH
     GGCPFDPAAA TLFATAGAQA
//

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