ID B9M948_GEODF Unreviewed; 637 AA.
AC B9M948;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Benzoyl-CoA reductase electron transfer protein, putative {ECO:0000313|EMBL:ACM18606.1};
GN Name=bamH-2 {ECO:0000313|EMBL:ACM18606.1};
GN OrderedLocusNames=Geob_0234 {ECO:0000313|EMBL:ACM18606.1};
OS Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS daltonii).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM18606.1, ECO:0000313|Proteomes:UP000007721};
RN [1] {ECO:0000313|EMBL:ACM18606.1, ECO:0000313|Proteomes:UP000007721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC {ECO:0000313|Proteomes:UP000007721};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kostka J., Richardson P.;
RT "Complete sequence of Geobacter sp. FRC-32.";
RL Submitted (JAN-2009) 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; CP001390; ACM18606.1; -; Genomic_DNA.
DR RefSeq; WP_012645335.1; NC_011979.1.
DR AlphaFoldDB; B9M948; -.
DR STRING; 316067.Geob_0234; -.
DR KEGG; geo:Geob_0234; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_3_2_7; -.
DR OrthoDB; 9805533at2; -.
DR Proteomes; UP000007721; 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; 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; 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.
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:UP000007721};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 557..586
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 587..616
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 637 AA; 68490 MW; E6D28C424EED4AC4 CRC64;
MAKINSTVEF EALRKEILSS RDPNRPCIAV CTGSGCLALG AAKLVAALKS EIKEQGLEQR
IEVRETGCPG FCERGPLIVI YPEETCYLKV QPTDAKEVIA SVMEKKIIDR LLYVDQVTGE
RVVHEMDIPF YKNQLRLLIG NNIKLDPTSI DDYIAIGGYT ALEKAVCQMK PEQVVGLVKE
SGLRGRGGGG FPSGNKWEFT RNAPDPVKYV VVNADEGDPG AFMDRALLEG SPHAVLEGLI
IGAYAIGAHE GFLYVRQEYP LAVHNITLAI QKAEEYGFLG KNILGSGFDF TVEVAQGAGA
FVCGEETALI RSLEGKTGEP KPRPPFPAVR GLWNKPTNIN NVETWANIPL IINKGPAAFA
SVGTGGSKGT KIFSLVGKVK NTGLVEVPMG ITLRDIVYKI GGGIPGEKKF KAVQTGGPAG
GCMPESLLDM EVDFDQLTKA GSMMGSGGMI VLDEETCMVD FARFFLSFLA EESCGKCVPC
REGIQQMLAI LNDLTHGKGK KGDLELLEQL TEVSSASLCA LGKGAPNPVL STLKHFRDEY
QAHMEGKCPA FTCKSLFSYY IEPEKCQACT SCGKKCPAGA IEGGKNQIHM VDQAKCTKCG
ACLQACPPRF AAVTRILGEV VPPPLPEEAR TIVRGSK
//
