ID A4J527_DESRM Unreviewed; 569 AA.
AC A4J527;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=NAD(P)-dependent iron-only hydrogenase diaphorase component flavoprotein {ECO:0000313|EMBL:ABO50180.1};
DE EC=1.6.99.5 {ECO:0000313|EMBL:ABO50180.1};
GN OrderedLocusNames=Dred_1652 {ECO:0000313|EMBL:ABO50180.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO50180.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO50180.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO50180.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
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., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
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DR EMBL; CP000612; ABO50180.1; -; Genomic_DNA.
DR RefSeq; WP_011877995.1; NC_009253.1.
DR AlphaFoldDB; A4J527; -.
DR STRING; 349161.Dred_1652; -.
DR KEGG; drm:Dred_1652; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_3_2_9; -.
DR OrthoDB; 9761899at2; -.
DR Proteomes; UP000001556; 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; 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; 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; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR Pfam; PF01257; 2Fe-2S_thioredx; 1.
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; 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; PS00645; COMPLEX1_51K_2; 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:ABO50180.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 464..509
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 569 AA; 61623 MW; 49D425CD0169D8AE CRC64;
MNFKELELLR ATAKEGIKLR LGEEPSDNFK YHVLVCGGTG CHSVGCQNTL QALQKAIDSQ
GLQDTVKLVV TGCMGTCEMG PVITVFPDGY YYCRVQPEDA EELVTSHLKE GKYVDRLCYH
TADGTVQPRK SDMTFFKKQK RNALRNCGLI NQTSIEEYIA VGGFKALAKT LQEMTPQQVV
DEVKKSGLRG RGGGGFPTGL KWQFVLDQKS DQKYVVCNGD EGDPGAFMDR SVLEDDPYSV
IEAMTIGGYA VGANKGYAYI RLEYPKAIDH FNKALARARE VGLLGNNILE SDFSFDIEIR
VGAGAFVCGE ETALLASIEG RRGEPRPRPP FPAVSGLFEK PTLLNNVETY ASICPIIING
GEWYATMGTE KSKGTKVFTL AGKINNTGLV EIPLGLTLRE MVEDIGGGVP NGKAFKAAQT
GGPSGGCIPA AYLDTPIDYE NLAALGSIVG SGGMIIVDES TCMVDLAKFY LGFTQDESCG
KCTPCRIGTK RMLEILERIT KGLGKPEDLD LLVELANSIK ASALCGLGQT APNPILSTLR
YFRDEFEAHI KDKTCPAGVC KMPRKGLKS
//
