SFRA_GEOSL
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 03-AUG-2022, entry version 122.
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., 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 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., 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: NADPH-dependent Fe(3+) reductase. Probably involved in
CC acetate metabolism and not in the reduction of Fe(3+) chelates. Unable
CC to utilize NADH or formate as electron donors. Unlike formate
CC dehydrogenases, contains no W, Mo or Se. Substrates are Fe(3+)-
CC nitrilotriacetate >> Fe(3+)-citrate or Fe(3+)-EDTA > Fe(3+)-
CC oxyhydroxide. Catalyzes also the reduction of NADP(+) with reduced
CC methyl viologen as electron donor. No activity with menadione as
CC electron acceptor. May be alternatively involved in transferring
CC electrons from reduced ferredoxin to NADP(+) and may serve as a major
CC 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 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 {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 inner membrane
CC {ECO:0000305|PubMed:17906154}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11443080, ECO:0000269|PubMed:17906154}.
CC -!- INDUCTION: Expressed constitutively. {ECO:0000269|PubMed:11443080}.
CC -!- MISCELLANEOUS: SfrA lacks the residues that are catalytically important
CC in formate dehydrogenases, including a Cys residue which is a ligand to
CC the heavy-metal atom (Mo or W) of the molybdopterin cofactor.
CC {ECO:0000305|PubMed:11443080}.
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; AAR33840.1; -; Genomic_DNA.
DR RefSeq; NP_951567.1; NC_002939.5.
DR RefSeq; WP_010941177.1; NC_002939.5.
DR AlphaFoldDB; Q74FU6; -.
DR SMR; Q74FU6; -.
DR STRING; 243231.GSU0509; -.
DR EnsemblBacteria; AAR33840; AAR33840; GSU0509.
DR KEGG; gsu:GSU0509; -.
DR PATRIC; fig|243231.5.peg.510; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_7; -.
DR InParanoid; Q74FU6; -.
DR OMA; HKNVGPL; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
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: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 GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
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 inner membrane; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..844
FT /note="NADPH-Fe(3+) oxidoreductase subunit alpha"
FT /id="PRO_0000429033"
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:0000255"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
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:0000255"
FT BINDING 149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 186
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 189
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
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
