GenomeNet

Database: UniProt
Entry: Q74FU6
LinkDB: Q74FU6
Original site: Q74FU6 
ID   SFRA_GEOSL              Reviewed;         844 AA.
AC   Q74FU6;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 108.
DE   RecName: Full=NADPH-Fe(3+) oxidoreductase subunit alpha;
DE            EC=1.-.-.-;
DE   AltName: Full=Soluble Fe(3+) reductase alpha subunit;
GN   Name=sfrA; OrderedLocusNames=GSU0509;
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.,
RA   Van Aken S.E., 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 1-20, FUNCTION, SUBCELLULAR LOCATION, INDUCTION,
RP   SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
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.,
RA   Nevin K.P., Woodard T.L., Liu A., Lovley D.R.;
RT   "Involvement of Geobacter sulfurreducens SfrAB in acetate metabolism
RT   rather than intracellular, respiration-linked Fe(III) citrate
RT   reduction.";
RL   Microbiology 153:3572-3585(2007).
CC   -!- FUNCTION: NADPH-dependent Fe(3+) reductase. Probably involved in
CC       acetate metabolism and not in the reduction of Fe(3+) chelates.
CC       Unable to utilize NADH or formate as electron donors. Unlike
CC       formate dehydrogenases, contains no W, Mo or Se. Substrates are
CC       Fe(3+)-nitrilotriacetate >> Fe(3+)-citrate or Fe(3+)-EDTA >
CC       Fe(3+)-oxyhydroxide. Catalyzes also the reduction of NADP(+) with
CC       reduced methyl viologen as electron donor. No activity with
CC       menadione as electron acceptor. May be alternatively involved in
CC       transferring electrons from reduced ferredoxin to NADP(+) and may
CC       serve as a major route for NADP regeneration.
CC       {ECO:0000269|PubMed:11443080, ECO:0000269|PubMed:17906154}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01184};
CC   -!- ACTIVITY REGULATION: Not regulated by FAD or FMN.
CC       {ECO:0000269|PubMed:11443080}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=25 uM for NADPH {ECO:0000269|PubMed:11443080};
CC         KM=1 mM for Fe(3+)-nitrilotriacetate
CC         {ECO:0000269|PubMed:11443080};
CC       pH dependence:
CC         Optimum pH is 5.5. {ECO:0000269|PubMed:11443080};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:11443080};
CC   -!- SUBUNIT: Heterotetramer with 2 beta subunits.
CC       {ECO:0000269|PubMed:11443080}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
CC       membrane protein.
CC   -!- INDUCTION: Expressed constitutively.
CC       {ECO:0000269|PubMed:11443080}.
CC   -!- MISCELLANEOUS: SfrA lacks the residues that are catalytically
CC       important in formate dehydrogenases, including a Cys residue which
CC       is a ligand to the heavy-metal atom (Mo or W) of the molybdopterin
CC       cofactor. {ECO:0000305|PubMed:11443080}.
CC   -!- CAUTION: PubMed:17906154 suggests that SfrAB is involved in
CC       acetate metabolism and does not participate directly in the
CC       reduction of Fe(3+) chelates, as was initially proposed in
CC       PubMed:11443080. {ECO:0000305}.
DR   EMBL; AE017180; AAR33840.1; -; Genomic_DNA.
DR   RefSeq; NP_951567.1; NC_002939.5.
DR   RefSeq; WP_010941177.1; NC_002939.5.
DR   ProteinModelPortal; Q74FU6; -.
DR   SMR; Q74FU6; -.
DR   STRING; 243231.GSU0509; -.
DR   EnsemblBacteria; AAR33840; AAR33840; GSU0509.
DR   GeneID; 2686077; -.
DR   KEGG; gsu:GSU0509; -.
DR   PATRIC; fig|243231.5.peg.510; -.
DR   eggNOG; ENOG4108IEG; Bacteria.
DR   eggNOG; COG3383; LUCA.
DR   HOGENOM; HOG000031440; -.
DR   InParanoid; Q74FU6; -.
DR   KO; K05299; -.
DR   OMA; QDQAMAY; -.
DR   BioCyc; GSUL243231:G1G0I-552-MONOMER; -.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IDA:TIGR.
DR   GO; GO:0009061; P:anaerobic respiration; TAS:TIGR.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR   InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR   Pfam; PF13237; Fer4_10; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS51839; 4FE4S_HC3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR   PROSITE; PS00642; COMPLEX1_75K_2; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 4Fe-4S; Cell membrane; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN         1    844       NADPH-Fe(3+) oxidoreductase subunit
FT                                alpha.
FT                                /FTId=PRO_0000429033.
FT   DOMAIN        1     78       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN       78    117       4Fe-4S His(Cys)3-ligated-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184}.
FT   DOMAIN      137    168       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      177    206       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      215    270       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01004}.
FT   COMPBIAS    461    486       Ala-rich.
FT   METAL        34     34       Iron-sulfur 1 (2Fe-2S). {ECO:0000255}.
FT   METAL        45     45       Iron-sulfur 1 (2Fe-2S). {ECO:0000255}.
FT   METAL        48     48       Iron-sulfur 1 (2Fe-2S). {ECO:0000255}.
FT   METAL        62     62       Iron-sulfur 1 (2Fe-2S). {ECO:0000255}.
FT   METAL        94     94       Iron-sulfur 2 (4Fe-4S); via tele
FT                                nitrogen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01184}.
FT   METAL        98     98       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184}.
FT   METAL       101    101       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184}.
FT   METAL       107    107       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184}.
FT   METAL       146    146       Iron-sulfur 3 (4Fe-4S). {ECO:0000255}.
FT   METAL       149    149       Iron-sulfur 3 (4Fe-4S). {ECO:0000255}.
FT   METAL       152    152       Iron-sulfur 3 (4Fe-4S). {ECO:0000255}.
FT   METAL       186    186       Iron-sulfur 4 (4Fe-4S). {ECO:0000255}.
FT   METAL       189    189       Iron-sulfur 4 (4Fe-4S). {ECO:0000255}.
FT   METAL       192    192       Iron-sulfur 4 (4Fe-4S). {ECO:0000255}.
FT   METAL       196    196       Iron-sulfur 4 (4Fe-4S). {ECO:0000255}.
FT   METAL       222    222       Iron-sulfur 5 (4Fe-4S). {ECO:0000255}.
FT   METAL       225    225       Iron-sulfur 5 (4Fe-4S). {ECO:0000255}.
FT   METAL       229    229       Iron-sulfur 5 (4Fe-4S). {ECO:0000255}.
FT   METAL       256    256       Iron-sulfur 5 (4Fe-4S). {ECO:0000255}.
SQ   SEQUENCE   844 AA;  89387 MW;  0418F261190FFA3B CRC64;
     MVSLTIDGKD ITVAKETTIL DAAALLGITI PTLCWLKKVS PTGACRVCAV EIEGVDRPMT
     ACNTPVKDGI KVTTQSEKLS RIRQKIMELM LVNHPLDCPV CDAGGECDLQ NACYGLGAAK
     QEYGAVLERR KIRYDWPLIE SDPNRCILCE KCVKVDHEIV GCNAIRVVNR GEATIIDTVD
     GNPLNCEFCG NCVAACPTGT LISKPFKFRG RPWAFTTTPS VCPFCATGCQ IEYHSRNGRV
     ERVTSDDSTY NSGNLCINGR FGYSYINSPD RLAEPMVKGQ KADWNTAMGT AATALKQIVA
     SHGADAVAGF GSPRVTNEDN YLFQKLMRSA IGTGNIDSEA RLGFAATQKV LREMLGIAGA
     STTIDAIDRA TAVLVVGCDL NAEATGMEYR VIKAATKNNA KLVLAAMRDI KLKKFANSHL
     KYRPGNETLL INALTKAVLE EGLENKEFCS ANISNLSDLT AALAGVSIAD AAAATGVTEA
     DLRAAARLVG GKKGVAVIFG AELMRGGNTD AVKALINLAL ILGATAGDTG GLFPVYEKTN
     IRGLLDMGVA PDHFPGHQTD GTTFEKAWGK KLPAAAGKDL WQIIEGIEQG SVKALYLLGC
     DPVASFPEGE RIRKALEKLE LLIVQDPFPG EAAKMAHVVF PSSVAAEKNG TFTTIDGRVQ
     PLAKAVAPSG DAREDWDILT ELYNRLTGES RIHSPAAVLD EVAALVPAYA SVGRTGGTIT
     AQPRSGGLAL APVSARAVAG SPTTLLVGTI LYHSGTTTTW SKNNLEIIPK GYIEIHPNDA
     AKLGIAEGGK VRLSAGSVKV EGTAKITPRV QPGLLFAPSH FRGMNVNALL SRDGGVVPVT
     VEKA
//
DBGET integrated database retrieval system