SFRA_GEOSK
ID SFRA_GEOSK Reviewed; 844 AA.
AC D7AF63;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=KN400_0498;
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: The SfrAB enzymatic complex is probably involved in acetate
CC metabolism and does not participate directly in the reduction of Fe(3+)
CC chelates. May serve as a major route for NADP regeneration.
CC {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. {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer with 2 beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:17906154}; Peripheral membrane protein
CC {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}.
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DR EMBL; CP002031; ADI83361.1; -; Genomic_DNA.
DR RefSeq; WP_010941177.1; NC_017454.1.
DR AlphaFoldDB; D7AF63; -.
DR SMR; D7AF63; -.
DR KEGG; gsk:KN400_0498; -.
DR PATRIC; fig|663917.3.peg.505; -.
DR HOGENOM; CLU_000422_4_0_7; -.
DR OMA; HKNVGPL; -.
DR OrthoDB; 323168at2; -.
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; IEA:UniProtKB-KW.
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: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 3: Inferred from homology;
KW 2Fe-2S; 4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Oxidoreductase; Repeat.
FT CHAIN 1..844
FT /note="NADPH-Fe(3+) oxidoreductase subunit alpha"
FT /id="PRO_0000429034"
FT DOMAIN 1..78
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 78..117
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT DOMAIN 137..168
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 177..206
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 215..270
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 34
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 98
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 101
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 146
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255"
FT BINDING 225
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255"
FT BINDING 229
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255"
FT BINDING 256
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="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
