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SFRB_GEOSL
ID   SFRB_GEOSL              Reviewed;         672 AA.
AC   Q74FU5;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=GSU0510;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-21, SUBCELLULAR LOCATION, SUBUNIT, AND FUNCTION.
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=11443080; DOI=10.1128/jb.183.15.4468-4476.2001;
RA   Kaufmann F., Lovley D.R.;
RT   "Isolation and characterization of a soluble NADPH-dependent Fe(III)
RT   reductase from Geobacter sulfurreducens.";
RL   J. Bacteriol. 183:4468-4476(2001).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
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: May catalyze the NADPH oxidation in the SfrAB NADPH-Fe(3+)
CC       oxidoreductase enzymatic complex. Probably involved in acetate
CC       metabolism and not in the reduction of Fe(3+) chelates. May serve as a
CC       major route for NADP regeneration. {ECO:0000269|PubMed:11443080,
CC       ECO:0000269|PubMed:17906154}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster.;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- SUBUNIT: Heterotetramer with 2 alpha subunits.
CC       {ECO:0000269|PubMed:11443080}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC       protein.
CC   -!- CAUTION: PubMed:17906154 suggests that SfrAB is involved in acetate
CC       metabolism and does not participate directly in the reduction of Fe(3+)
CC       chelates, as was initially proposed in PubMed:11443080. {ECO:0000305}.
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DR   EMBL; AE017180; AAR33841.1; -; Genomic_DNA.
DR   RefSeq; NP_951568.1; NC_002939.5.
DR   RefSeq; WP_010941178.1; NC_002939.5.
DR   AlphaFoldDB; Q74FU5; -.
DR   SMR; Q74FU5; -.
DR   STRING; 243231.GSU0510; -.
DR   EnsemblBacteria; AAR33841; AAR33841; GSU0510.
DR   KEGG; gsu:GSU0510; -.
DR   PATRIC; fig|243231.5.peg.511; -.
DR   eggNOG; COG0493; Bacteria.
DR   eggNOG; COG1894; Bacteria.
DR   HOGENOM; CLU_000422_3_4_7; -.
DR   InParanoid; Q74FU5; -.
DR   OMA; MGRVCPA; -.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IDA:TIGR.
DR   GO; GO:0009061; P:anaerobic respiration; TAS:TIGR.
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   1: Evidence at protein level;
KW   4Fe-4S; Cell membrane; Cytoplasm; Direct protein sequencing; FAD;
KW   Flavoprotein; Iron; Iron-sulfur; Membrane; Metal-binding; NADP;
KW   Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11443080"
FT   CHAIN           2..672
FT                   /note="NADPH-Fe(3+) oxidoreductase subunit beta"
FT                   /id="PRO_0000429035"
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
 
 
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