ID E1QE74_DESB2 Unreviewed; 641 AA.
AC E1QE74;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ADK83860.1};
GN OrderedLocusNames=Deba_0487 {ECO:0000313|EMBL:ADK83860.1};
OS Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS / 2st14).
OC Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC Desulfarculaceae; Desulfarculus.
OX NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK83860.1, ECO:0000313|Proteomes:UP000009047};
RN [1] {ECO:0000313|EMBL:ADK83860.1, ECO:0000313|Proteomes:UP000009047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC {ECO:0000313|Proteomes:UP000009047};
RX PubMed=21304732; DOI=10.4056/sigs.1243258;
RA Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL Stand. Genomic Sci. 3:276-284(2010).
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DR EMBL; CP002085; ADK83860.1; -; Genomic_DNA.
DR AlphaFoldDB; E1QE74; -.
DR STRING; 644282.Deba_0487; -.
DR KEGG; dbr:Deba_0487; -.
DR eggNOG; COG0493; Bacteria.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_000422_3_4_7; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000009047; 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 Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 2.
DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000009047}.
FT DOMAIN 53..98
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 641 AA; 69572 MW; 90045A5E409E45A8 CRC64;
MASQVFSTWG SWTPGREQVP TDQLPAEFAA GRPLRAFMGW DGLFIHDESV DLVDMARAYM
DQAQKESCGQ CFPCRLGVKA MSAILDGLCA GKGAPADLDR LESLARFVSR ASRCDIGQTT
PRPILDLLTH RRQAFLAAIE AKAPIARGRY VAQVTAPCIN ACPSHLDIPG YVEKIRDGRW
DQALSIIRDD CCLPGVVGRV CVRPCEFNCR RQKLDEGIAI RALKRHAADM ELASGREAPL
VPGPAKEQKV AIIGAGPAGL ACAYHLGLRG YKSTIFEVLN EPGGMAAVGI PDYRLPRRIL
RGEANQVERL GCEIRYGVNV GVDVTLDDLK LQGYGAIFVG VGAPAASKMR CEGEDAGYEC
FMTGVDFLRR VADGERPIEG DKLLIIGGGN VAMDCARSAL RLGFTDVNLL YRRTRAEMPA
DLVEISEAQE EGIKFHYLVA PLRVIAANGK VAGLECQRME LGEPDASGRR RPVAIEGSEF
VIECDAIVPA IGQVCVVDCV LPPDEVEISR RNTLATDDIT RQTNQPYIFS GGDCVTGPAP
LIAALDAGKN AARFIEQFLT NGRSVPEDGD HMERLIARLG VFYPREKMPY ADATKKLRPP
VMAPEVRIRG FDEVEGGVSP AQAAEEAARC LRCYRIAMAA L
//
