ID C0BZ71_9FIRM Unreviewed; 595 AA.
AC C0BZ71;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=4Fe-4S binding domain protein {ECO:0000313|EMBL:EEG74449.1};
GN ORFNames=CLOHYLEM_05110 {ECO:0000313|EMBL:EEG74449.1};
OS [Clostridium] hylemonae DSM 15053.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=553973 {ECO:0000313|EMBL:EEG74449.1, ECO:0000313|Proteomes:UP000004893};
RN [1] {ECO:0000313|EMBL:EEG74449.1, ECO:0000313|Proteomes:UP000004893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG74449.1,
RC ECO:0000313|Proteomes:UP000004893};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium hylemonae (DSM 15053).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG74449.1, ECO:0000313|Proteomes:UP000004893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG74449.1,
RC ECO:0000313|Proteomes:UP000004893};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2009) 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:EEG74449.1}.
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DR EMBL; ABYI02000019; EEG74449.1; -; Genomic_DNA.
DR RefSeq; WP_006442446.1; NZ_GG657759.1.
DR AlphaFoldDB; C0BZ71; -.
DR STRING; 553973.CLOHYLEM_05110; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_3_2_9; -.
DR OrthoDB; 9761899at2; -.
DR Proteomes; UP000004893; 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; -; 2.
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 Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 538..567
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 568..595
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 595 AA; 64698 MW; BF88E0E5F9F4AFDA CRC64;
MYRSHVLVCG GTGCTSSGSQ KIRERLEAEI KRNGLEDEVG VVKTGCFGLC ALGPIMIVYP
EGSFYAMVKE EDIPEIVSEH LLKGRVVTRL LYDETVKNEE VLPLQETKFY KKQHRVALRN
CGVINPENIE EYIGTRGYEA LGTVLTSMKP EEVIQVILDS GLRGRGGAGF PTGLKWKFAA
ANEADQKYVC CNADEGDPGA FMDRSVLEGD PHVVLEAMAI AGYAIGASQG YIYVRAEYPI
AVERLNIAIE QAREYGLLGK NIFETGFDFD IDIRLGAGAF VCGEETALMT SIEGNRGEPR
PRPPFPALKG LFQKPTILNN VETLANIPQI ILNGAEWFSS MGTEKSKGTK VFALGGKVNN
TGLVEIPMGT TLREIVEEIG GGIPNGKKFK AAQTGGPSGG CIPAEHFDVP IDYDNLIAIG
SMMGSGGLIV MDEDNCMVDI AKFFLEFTVD ESCGKCTPCR VGTRRMLEIL EKITNGQGTM
EDLDKLEELA AHLKTNSLCA LGQTAPNPVL STMRYFRDEY VAHIVDKKCP AGVCKALLSY
KIDADKCKGC TLCARTCPND AISGAVKEPH VIHQDKCVKC GACMEKCRFG AIYKE
//
