GenomeNet

Database: UniProt
Entry: A9BFV2_PETMO
LinkDB: A9BFV2_PETMO
Original site: A9BFV2_PETMO 
ID   A9BFV2_PETMO            Unreviewed;       485 AA.
AC   A9BFV2;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:ABX31448.1};
DE            EC=1.6.99.5 {ECO:0000313|EMBL:ABX31448.1};
GN   OrderedLocusNames=Pmob_0724 {ECO:0000313|EMBL:ABX31448.1};
OS   Petrotoga mobilis (strain DSM 10674 / SJ95).
OC   Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC   Petrotoga.
OX   NCBI_TaxID=403833 {ECO:0000313|EMBL:ABX31448.1, ECO:0000313|Proteomes:UP000000789};
RN   [1] {ECO:0000313|EMBL:ABX31448.1, ECO:0000313|Proteomes:UP000000789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10674 / SJ95 {ECO:0000313|Proteomes:UP000000789};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Noll K., Richardson P.;
RT   "Complete sequence of Petroga mobilis SJ95.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00007523}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000879; ABX31448.1; -; Genomic_DNA.
DR   RefSeq; WP_012208551.1; NC_010003.1.
DR   AlphaFoldDB; A9BFV2; -.
DR   STRING; 403833.Pmob_0724; -.
DR   KEGG; pmo:Pmob_0724; -.
DR   eggNOG; COG1894; Bacteria.
DR   HOGENOM; CLU_014881_3_2_0; -.
DR   OrthoDB; 9761899at2; -.
DR   Proteomes; UP000000789; Chromosome.
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   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 6.10.250.1450; -; 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; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_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   PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF13187; Fer4_9; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   Pfam; PF10531; SLBB; 1.
DR   SMART; SM00928; NADH_4Fe-4S; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 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   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
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   Oxidoreductase {ECO:0000313|EMBL:ABX31448.1};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          428..457
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          458..485
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   485 AA;  52548 MW;  30FAF7B160A60C5E CRC64;
     MPEQVRIVLR NAGNIDPENI EDYLKNNGYL ALAKALNSKR EEVIQTVLDS NLRGRGGGGF
     PTGLKWKFAM QAKGDEKYVI CNADEGDPGA FMDRSVLEGD PHSVLEGMAI AGYAIGAQKG
     IIYIRAEYPL AVARLKVAIS QAKDYGLLGE NILGSNFSFD IEIRLGAGAF VCGEETALIH
     SIEGLRGEPT NKPPFPANSG LWKKPTVINN VETLANIAPI ILNGADWFKQ FGTENSPGTK
     VFALAGDVKK VGLVEVPMGT TLREIIFDIG GGIKGDKKFK AVQTGGPSGG CIPAEYLDTP
     IDYDSLQALG SMMGSGGMIV MDEDTCMVDV AKFYLQFTVD ESCGKCTTCR VGNVRLLEIL
     EKITSGNAQL EDLDHMLTLA NVVKNGSLCG LGQTAPNPIL STYRYFEDEY KEHILDRNCR
     AGVCKNLIRY EIIPENCTGC TACARVCPTE AIQGELRKPH TIDQEKCIKC GSCYTTCRFN
     AIKIV
//
DBGET integrated database retrieval system