ID F2NHM1_DESAR Unreviewed; 617 AA.
AC F2NHM1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:AEB09208.1};
DE EC=1.6.99.5 {ECO:0000313|EMBL:AEB09208.1};
GN OrderedLocusNames=Desac_1351 {ECO:0000313|EMBL:AEB09208.1};
OS Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2).
OC Bacteria; Thermodesulfobacteriota; Desulfobaccia; Desulfobaccales;
OC Desulfobaccaceae; Desulfobacca.
OX NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB09208.1, ECO:0000313|Proteomes:UP000000483};
RN [1] {ECO:0000313|EMBL:AEB09208.1, ECO:0000313|Proteomes:UP000000483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC {ECO:0000313|Proteomes:UP000000483};
RX PubMed=21886866;
RA Goker M., Teshima H., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of the acetate-degrading sulfate reducer
RT Desulfobacca acetoxidans type strain (ASRB2).";
RL Stand. Genomic Sci. 4:393-401(2011).
RN [2] {ECO:0000313|Proteomes:UP000000483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC {ECO:0000313|Proteomes:UP000000483};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Desulfobacca acetoxidans DSM 11109.";
RL Submitted (MAR-2011) 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; CP002629; AEB09208.1; -; Genomic_DNA.
DR RefSeq; WP_013706320.1; NC_015388.1.
DR AlphaFoldDB; F2NHM1; -.
DR STRING; 880072.Desac_1351; -.
DR KEGG; dao:Desac_1351; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_3_2_7; -.
DR OrthoDB; 9805533at2; -.
DR Proteomes; UP000000483; Chromosome.
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; 3.30.70.20; -; 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; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; IPR036249; Thioredoxin-like_sf.
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 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 SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:AEB09208.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000483}.
FT DOMAIN 560..589
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 590..617
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 617 AA; 67180 MW; 9A5E11078DB5775C CRC64;
MPFIESIDHL TEYRRLVRAK RDPNQLQVLV CGGPGCLPLG SEELVAAFKA EMEAKGIDGK
VILKTTGCHG LCSHGVRVLI RPQEIAYQKV QPEDVAEIVD LTLINGGLVE RLLYQDPIDG
KFCPHKADIP FYQTQNPLVL RKLDAIDPES LDDYLALGGY RTLRKILFQM TPERVIDQVE
KSGLRGRGGG GFLTGRKWRL CRQVPGEVKF IICNGDEGDP GAFMDRAVME GDPHAVIEGL
IVGAYAIGAL KGYIYVRHEY PLAVKRLTRA VEQARDFGFL GTNILRSKFS FDIKISQGAG
AFVCGEETAL IASIEGRIGE PMPRPPYPIQ AGLFGLPTVI NNVETLANIP EIINLGAEHF
AALGTEKSKG TKVFSLVGAV NNTGLLEVPM GTSLRHIVYD LGGGIPGNHE FKAVQTGGPS
GGCIPKQFLD LPVDYDSLQQ VGSIMGSGGM IVMDTKSCMV DVARYFISFL MQESCGKCTP
CREGLKQLHA ILTDITSGRG EEKHLAMMED LCRTMASASL CGLGQSAANP VLSTLKYFRE
EYTKHIVDKK CPALVCRQLL TYTIDPNECT SCLACVRECP VGAISGPKKE PQVINQDLCI
KCGLCHDVCQ FDAVKVE
//