FERCR_ARCFU
ID FERCR_ARCFU Reviewed; 169 AA.
AC O29428;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Ferric-chelate reductase (NAD(P)H) {ECO:0000305};
DE EC=1.16.1.10 {ECO:0000269|PubMed:10593977};
GN Name=feR {ECO:0000303|PubMed:11525168};
GN OrderedLocusNames=AF_0830 {ECO:0000312|EMBL:AAB90418.1};
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325 {ECO:0000312|EMBL:AAB90418.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP PROTEIN SEQUENCE OF 1-19, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10593977; DOI=10.1074/jbc.274.51.36715;
RA Vadas A., Monbouquette H.G., Johnson E., Schroeder I.;
RT "Identification and characterization of a novel ferric reductase from the
RT hyperthermophilic Archaeon Archaeoglobus fulgidus.";
RL J. Biol. Chem. 274:36715-36721(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH FMN AND NADP, AND
RP SUBUNIT.
RX PubMed=11525168; DOI=10.1016/s0969-2126(01)00589-5;
RA Chiu H.J., Johnson E., Schroder I., Rees D.C.;
RT "Crystal structures of a novel ferric reductase from the hyperthermophilic
RT archaeon Archaeoglobus fulgidus and its complex with NADP+.";
RL Structure 9:311-319(2001).
CC -!- FUNCTION: Catalyzes the reduction of bound ferric iron (Fe(3+)) in a
CC variety of iron chelators (siderophores) using NAD(P)H as the electron
CC donor, resulting in the release of Fe(2+). Not active with uncomplexed
CC Fe(3+). Also reduces FMN and FAD, but not riboflavin.
CC {ECO:0000269|PubMed:10593977}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-
CC siderophore + NADH; Xref=Rhea:RHEA:15061, Rhea:RHEA-COMP:11342,
CC Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.16.1.10; Evidence={ECO:0000269|PubMed:10593977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-
CC siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342,
CC Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.16.1.10; Evidence={ECO:0000269|PubMed:10593977};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:10593977};
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10593977};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=61 uM for NADH (with Fe(+3) as acceptor)
CC {ECO:0000269|PubMed:10593977};
CC KM=80 uM for NAD(P)H (with Fe(+3) as acceptor)
CC {ECO:0000269|PubMed:10593977};
CC KM=66 uM for Fe(+3) (with NAD(P)H as donor)
CC {ECO:0000269|PubMed:10593977};
CC KM=0.3 uM for FMN (with NAD(P)H as donor)
CC {ECO:0000269|PubMed:10593977};
CC Vmax=4935 umol/min/mg enzyme with NADH as donor and Fe(3+) as
CC acceptor {ECO:0000269|PubMed:10593977};
CC Vmax=3505 umol/min/mg enzyme with NAD(P)H as donor and Fe(3+) as
CC acceptor {ECO:0000269|PubMed:10593977};
CC Vmax=280 umol/min/mg enzyme with NAD(P)H as donor and FMN as acceptor
CC {ECO:0000269|PubMed:10593977};
CC Vmax=350 umol/min/mg enzyme with NAD(P)H as donor and FAD as acceptor
CC {ECO:0000269|PubMed:10593977};
CC Temperature dependence:
CC Optimum temperature is 88 degrees Celsius.
CC {ECO:0000269|PubMed:10593977};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11525168,
CC ECO:0000303|PubMed:10593977}.
CC -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC {ECO:0000305}.
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DR EMBL; AE000782; AAB90418.1; -; Genomic_DNA.
DR PIR; F69353; F69353.
DR RefSeq; WP_010878333.1; NC_000917.1.
DR PDB; 1I0R; X-ray; 1.50 A; A/B=1-169.
DR PDB; 1I0S; X-ray; 1.65 A; A/B=1-169.
DR PDBsum; 1I0R; -.
DR PDBsum; 1I0S; -.
DR AlphaFoldDB; O29428; -.
DR SMR; O29428; -.
DR STRING; 224325.AF_0830; -.
DR EnsemblBacteria; AAB90418; AAB90418; AF_0830.
DR GeneID; 1484049; -.
DR KEGG; afu:AF_0830; -.
DR eggNOG; arCOG02017; Archaea.
DR HOGENOM; CLU_059021_4_1_2; -.
DR OMA; CANTCFQ; -.
DR OrthoDB; 76604at2157; -.
DR PhylomeDB; O29428; -.
DR BRENDA; 1.16.1.10; 414.
DR EvolutionaryTrace; O29428; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0140618; F:ferric-chelate reductase (NADH) activity; IEA:RHEA.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:RHEA.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0016723; F:oxidoreductase activity, acting on metal ions, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR Gene3D; 2.30.110.10; -; 1.
DR InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR Pfam; PF01613; Flavin_Reduct; 1.
DR SMART; SM00903; Flavin_Reduct; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Flavoprotein; FMN; NADP;
KW Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..169
FT /note="Ferric-chelate reductase (NAD(P)H)"
FT /id="PRO_0000430711"
FT BINDING 7
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11525168,
FT ECO:0007744|PDB:1I0S"
FT BINDING 27..31
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:11525168,
FT ECO:0007744|PDB:1I0R, ECO:0007744|PDB:1I0S"
FT BINDING 45..52
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:11525168,
FT ECO:0007744|PDB:1I0R, ECO:0007744|PDB:1I0S"
FT BINDING 82..84
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:11525168,
FT ECO:0007744|PDB:1I0R, ECO:0007744|PDB:1I0S"
FT BINDING 89
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:11525168,
FT ECO:0007744|PDB:1I0R, ECO:0007744|PDB:1I0S"
FT BINDING 126
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11525168,
FT ECO:0007744|PDB:1I0S"
FT BINDING 147..154
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11525168,
FT ECO:0007744|PDB:1I0S"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:1I0R"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1I0R"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:1I0R"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1I0R"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:1I0R"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:1I0R"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:1I0R"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:1I0R"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:1I0R"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:1I0R"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:1I0R"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1I0R"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1I0R"
FT STRAND 109..122
FT /evidence="ECO:0007829|PDB:1I0R"
FT STRAND 124..138
FT /evidence="ECO:0007829|PDB:1I0R"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:1I0R"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1I0R"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1I0R"
SQ SEQUENCE 169 AA; 18659 MW; D23950527048DEA9 CRC64;
MDVEAFYKIS YGLYIVTSES NGRKCGQIAN TVFQLTSKPV QIAVCLNKEN DTHNAVKESG
AFGVSVLELE TPMEFIGRFG FRKSSEFEKF DGVEYKTGKT GVPLVTQHAV AVIEAKVVKE
CDVGTHTLFV GEAVDAEVLK DAEVLTYADY HLMKKGKTPR TATVYFESK
