ID A0A011VU56_RUMAL Unreviewed; 630 AA.
AC A0A011VU56;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:EXM38801.1};
GN ORFNames=RASY3_10595 {ECO:0000313|EMBL:EXM38801.1}, RASY3_19285
GN {ECO:0000313|EMBL:EXM38330.1};
OS Ruminococcus albus SY3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1341156 {ECO:0000313|EMBL:EXM38801.1, ECO:0000313|Proteomes:UP000021369};
RN [1] {ECO:0000313|EMBL:EXM38801.1, ECO:0000313|Proteomes:UP000021369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY3 {ECO:0000313|EMBL:EXM38801.1,
RC ECO:0000313|Proteomes:UP000021369};
RA Dassa B., Borovok I., Lamed R., Flint H., Yeoman C.J., White B.,
RA Bayer E.A.;
RT "Rumen cellulosomics: divergent fiber-degrading strategies revealed by
RT comparative genome-wide analysis of six Ruminococcal strains.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXM38801.1}.
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DR EMBL; JEOB01000004; EXM38330.1; -; Genomic_DNA.
DR EMBL; JEOB01000003; EXM38801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011VU56; -.
DR PATRIC; fig|1341156.4.peg.2064; -.
DR OrthoDB; 9761899at2; -.
DR Proteomes; UP000021369; Unassembled WGS sequence.
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; 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; PF00037; Fer4; 2.
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.
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 Reference proteome {ECO:0000313|Proteomes:UP000021369};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 573..602
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 603..630
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 630 AA; 67918 MW; CCFF1E83D04335FB CRC64;
MTIEELNKIK AAKADIVKVR TIIAEEGEKL AKETGYRKQV LVCGGTGCQS SHSMDVLKAL
KDELAAKGIA DEVLVVRTGC FGLCSLGPIV IVYPEGAFYA QATPEGIKRI VDEHLVNGEI
CKDLLYQETV HEDGSIISLY ETNFYRKQKR IALRNCGVID PEDIEEYIAT DGYQALYKAL
TSMTPDEVVK EVLDSGIRGR GGAGFPTGRK WMFTKDAPGD IKYVACNADE GDPGAFMDRS
ILEGDPHAVI EAMTIASYAV GAHQGYVYVR AEYPVAVNRL QIALDQAREY GLLGKDILGT
GHDFDIEIRL GAGAFVCGEE TALLTSIEGN RGEPRPRPPF PAVKGLFGKP TLLNNVETYA
NIAQIIRKGA AWYSSMGTEK SKGTKVFALG GKITNVGLVE IPMGTTLREI IEEIGGGIPD
GKAFKAAQTG GPSGGCIPAQ HIDTPIDYES LAALGSMMGS GGLIVMDEDN CMVDVSKFYL
NFTVDESCGK CTPCRVGTRK LLQLLEKITD GKGEMEDLEK IQDLATHMKS SSLCALGQSA
PNPVLSTLQY FGDEYLAHIK DKKCPAGVCK NLLQYEIIAD KCKGCTLCAR NCPANAITGT
VKNPHVIDTT KCIKCGVCMN NCKFGAIIKK
//
