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Database: UniProt
Entry: C8W2X2_DESAS
LinkDB: C8W2X2_DESAS
Original site: C8W2X2_DESAS 
ID   C8W2X2_DESAS            Unreviewed;       597 AA.
AC   C8W2X2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:ACV61128.1};
DE            EC=1.6.99.5 {ECO:0000313|EMBL:ACV61128.1};
GN   OrderedLocusNames=Dtox_0173 {ECO:0000313|EMBL:ACV61128.1};
OS   Desulfofarcimen acetoxidans (strain ATCC 49208 / DSM 771 / KCTC 5769 / VKM
OS   B-1644 / 5575) (Desulfotomaculum acetoxidans).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61128.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61128.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA   Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00007523}.
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DR   EMBL; CP001720; ACV61128.1; -; Genomic_DNA.
DR   RefSeq; WP_012813580.1; NC_013216.1.
DR   AlphaFoldDB; C8W2X2; -.
DR   STRING; 485916.Dtox_0173; -.
DR   KEGG; dae:Dtox_0173; -.
DR   eggNOG; COG1894; Bacteria.
DR   HOGENOM; CLU_014881_3_2_9; -.
DR   OMA; CVVRAVT; -.
DR   OrthoDB; 9761899at2; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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; IPR019554; Soluble_ligand-bd.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43578:SF3; HYDROGENASE SUBUNIT; 1.
DR   PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   Pfam; PF01257; 2Fe-2S_thioredx; 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   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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   Oxidoreductase {ECO:0000313|EMBL:ACV61128.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          540..569
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          570..597
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   597 AA;  64337 MW;  AAA653F22D78B362 CRC64;
     MSMYRSHVLV CAGAGCISSD CKAVQSALIA NIQAQGLKDE IKVVETGCMG PCDLGPVVLI
     FPDGVFYRKL KPEDTADIVT EHLLKGKLVD RLLHRPTGKS EQVATFDRME FFKRQTRVTL
     RNTGLINPES IEEYIARDGY QALGKVLSKY SPEEVISAIK ASGLRGRGGA GFPTGLKWEF
     TARASGNPKY VVCNADEGDP GAFMDRSILE GDPHSVLEAM AICGYAIGAE KGFIYVRAEY
     PLAVQRLETA IGKCLEYGLL GRNIFSTGFN FDIEIRVGAG AFVCGEETAL LASIEGRRGE
     PRPKPPFPAQ EGLWGKPTVI NNVETWANIP PIILNGPEWF SAIGTENSKG TKVFALAGKI
     NNTGLVEVPM GTPLKEIIYD IGGGIPNGKK FKAVQTGGPS GGCIPAEYLD TPVDYDSLVK
     LGTIMGSGGM IIVDEDTCMV DLAKFFLEFV QEESCGKCAP CRIGTKRMLE IMERIVEGNG
     KDGDIELLEE LSQGIKSSAL CGLGQTAPNP VLSTLRHFRE EYIAHIKDKR CPAGACQALV
     TYYIDARACK GCGLCSKNCP AGAISGEKKK PHVIDAGKCI KCGTCKDKCK FNSIFIL
//
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