SFRB_GEOSK
ID SFRB_GEOSK Reviewed; 672 AA.
AC D7AF64;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=NADPH-Fe(3+) oxidoreductase subunit beta;
DE EC=1.-.-.-;
DE AltName: Full=Soluble Fe(3+) reductase beta subunit;
GN Name=sfrB; OrderedLocusNames=KN400_0499;
OS Geobacter sulfurreducens (strain DL-1 / KN400).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=663917;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-1 / KN400;
RX PubMed=20544019; DOI=10.1371/journal.pone.0010922;
RA Nagarajan H., Butler J.E., Klimes A., Qiu Y., Zengler K., Ward J.,
RA Young N.D., Methe B.A., Palsson B.O., Lovley D.R., Barrett C.L.;
RT "De Novo assembly of the complete genome of an enhanced electricity-
RT producing variant of Geobacter sulfurreducens using only short reads.";
RL PLoS ONE 5:E10922-E10922(2010).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DL-1 / KN400;
RX PubMed=17906154; DOI=10.1099/mic.0.2007/006478-0;
RA Coppi M.V., O'neil R.A., Leang C., Kaufmann F., Methe B.A., Nevin K.P.,
RA Woodard T.L., Liu A., Lovley D.R.;
RT "Involvement of Geobacter sulfurreducens SfrAB in acetate metabolism rather
RT than intracellular, respiration-linked Fe(III) citrate reduction.";
RL Microbiology 153:3572-3585(2007).
CC -!- FUNCTION: Probably involved in acetate metabolism and not in the
CC reduction of Fe(3+) chelates. May serve as a major route for NADP
CC regeneration. {ECO:0000269|PubMed:17906154}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBUNIT: Heterotetramer with 2 alpha subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17906154};
CC Peripheral membrane protein {ECO:0000269|PubMed:17906154}.
CC -!- DISRUPTION PHENOTYPE: SfrAB-null strain is unable to grow in the
CC presence of acetate and fumarate unless an additional electron donor is
CC present. Strongly reduced NADPH-dependent benzyl viologen reductase
CC activity. {ECO:0000269|PubMed:17906154}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002031; ADI83362.1; -; Genomic_DNA.
DR RefSeq; WP_010941178.1; NC_017454.1.
DR AlphaFoldDB; D7AF64; -.
DR SMR; D7AF64; -.
DR KEGG; gsk:KN400_0499; -.
DR PATRIC; fig|663917.3.peg.506; -.
DR HOGENOM; CLU_000422_3_4_7; -.
DR OMA; MGRVCPA; -.
DR OrthoDB; 323168at2; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 3.50.50.60; -; 3.
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; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF140490; SSF140490; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cell membrane; FAD; Flavoprotein; Iron; Iron-sulfur; Membrane;
KW Metal-binding; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..672
FT /note="NADPH-Fe(3+) oxidoreductase subunit beta"
FT /id="PRO_0000429036"
FT BINDING 203
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 207
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 211
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 215
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 254..283
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 388..421
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 552..562
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 672 AA; 74273 MW; 3779DF2F9AE0D446 CRC64;
MAQVVFSSWG RTIVDNRKGG EAQDVSFRLP TTLDGERQIA AFMGWDGIIL YDLKVDVPAM
AAEYMKRVQT QYCCGKCTPG KKGTKVLADV LAAIIEGRAT EADLDTIDDL ADLLTNCKCT
LCQSSTIPVL DAVKHFREDF LAYITGIRKP ANVHRFIDKY TAPCMDRCPA HIDIPAYIEA
IKEYRFDESL DIIRDNMPLP SVCGRVCPHP CETHCRRKNV DDSVNIMVLK RSASDYEWMH
NAAPPMQPKP QKNKKVAIVG AGPAGLACAY YLALEGYPCT IYEALPEGYG GGMIAVGIPP
YRQPRHLLQR DIDIISSMGV DIIYDTRIGK DISLEELKQK FDAVFLAPGA HRSKPMGVEG
EDKGYKGFLK GGIDFLREAY MGRPTGMGKK VVVVGGGNTA IDCVRVALRE GAEESTLLYR
RSRKEMPADV WEVDGADEEG VRFEFQVLPT RVLVDENEQV TGVECVRMAL GEPDASGRRR
PEPVPGSEFV VECDTVIPAI GQDPDLSFIP DNLGIDITKW NTVVTKYVPL KDAAGKDLKD
GMGNPLARVL ITDLEGVFAG GDAEIGPLTV VACIGNAHRA ARVIQRWLEE GKAYLTEDEL
MEDILTNMPV YDKNEKVPWL DSRERAHQAE VHGQERASKG NYQEVELGFV DTQAVEEAER
CLRCYRVAMA AI
