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Ferric-chelate reductase (NAD(P)H) (EC 1.16.1.10)

 FERCR_ARCFU             Reviewed;         169 AA.
O29428;
29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
28-FEB-2018, entry version 98.
RecName: Full=Ferric-chelate reductase (NAD(P)H) {ECO:0000305};
EC=1.16.1.10 {ECO:0000269|PubMed:10593977};
Name=feR {ECO:0000303|PubMed:11525168};
OrderedLocusNames=AF_0830 {ECO:0000312|EMBL:AAB90418.1};
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM
9628 / NBRC 100126).
Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
Archaeoglobaceae; Archaeoglobus.
NCBI_TaxID=224325 {ECO:0000312|EMBL:AAB90418.1};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
PubMed=9389475; DOI=10.1038/37052;
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
Woese C.R., Venter J.C.;
"The complete genome sequence of the hyperthermophilic, sulphate-
reducing archaeon Archaeoglobus fulgidus.";
Nature 390:364-370(1997).
[2]
PROTEIN SEQUENCE OF 1-19, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10593977; DOI=10.1074/jbc.274.51.36715;
Vadas A., Monbouquette H.G., Johnson E., Schroeder I.;
"Identification and characterization of a novel ferric reductase from
the hyperthermophilic Archaeon Archaeoglobus fulgidus.";
J. Biol. Chem. 274:36715-36721(1999).
[3]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH FMN AND NADP,
AND SUBUNIT.
PubMed=11525168; DOI=10.1016/S0969-2126(01)00589-5;
Chiu H.J., Johnson E., Schroder I., Rees D.C.;
"Crystal structures of a novel ferric reductase from the
hyperthermophilic archaeon Archaeoglobus fulgidus and its complex with
NADP+.";
Structure 9:311-319(2001).
-!- FUNCTION: Catalyzes the reduction of bound ferric iron (Fe(3+)) in
a variety of iron chelators (siderophores) using NAD(P)H as the
electron donor, resulting in the release of Fe(2+). Not active
with uncomplexed Fe(3+). Also reduces FMN and FAD, but not
riboflavin. {ECO:0000269|PubMed:10593977}.
-!- CATALYTIC ACTIVITY: 2 Fe(II)-siderophore + NAD(P)(+) + H(+) = 2
Fe(III)-siderophore + NAD(P)H. {ECO:0000269|PubMed:10593977}.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:10593977};
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:10593977};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=61 uM for NADH (with Fe(+3) as acceptor)
{ECO:0000269|PubMed:10593977};
KM=80 uM for NAD(P)H (with Fe(+3) as acceptor)
{ECO:0000269|PubMed:10593977};
KM=66 uM for Fe(+3) (with NAD(P)H as donor)
{ECO:0000269|PubMed:10593977};
KM=0.3 uM for FMN (with NAD(P)H as donor)
{ECO:0000269|PubMed:10593977};
Vmax=4935 umol/min/mg enzyme with NADH as donor and Fe(3+) as
acceptor {ECO:0000269|PubMed:10593977};
Vmax=3505 umol/min/mg enzyme with NAD(P)H as donor and Fe(3+) as
acceptor {ECO:0000269|PubMed:10593977};
Vmax=280 umol/min/mg enzyme with with NAD(P)H as donor and FMN
as acceptor {ECO:0000269|PubMed:10593977};
Vmax=350 umol/min/mg enzyme with with NAD(P)H as donor and FAD
as acceptor {ECO:0000269|PubMed:10593977};
Temperature dependence:
Optimum temperature is 88 degrees Celsius.
{ECO:0000269|PubMed:10593977};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11525168,
ECO:0000303|PubMed:10593977}.
-!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase
family. {ECO:0000305}.
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EMBL; AE000782; AAB90418.1; -; Genomic_DNA.
PIR; F69353; F69353.
RefSeq; WP_010878333.1; NC_000917.1.
PDB; 1I0R; X-ray; 1.50 A; A/B=1-169.
PDB; 1I0S; X-ray; 1.65 A; A/B=1-169.
PDBsum; 1I0R; -.
PDBsum; 1I0S; -.
ProteinModelPortal; O29428; -.
SMR; O29428; -.
STRING; 224325.AF0830; -.
EnsemblBacteria; AAB90418; AAB90418; AF_0830.
GeneID; 1484049; -.
KEGG; afu:AF_0830; -.
eggNOG; arCOG02017; Archaea.
eggNOG; COG1853; LUCA.
KO; K18915; -.
OMA; NYTHELI; -.
OrthoDB; POG093Z0DY2; -.
BioCyc; AFUL224325:G1G17-856-MONOMER; -.
BRENDA; 1.16.1.10; 414.
EvolutionaryTrace; O29428; -.
Proteomes; UP000002199; Chromosome.
GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
GO; GO:0016723; F:oxidoreductase activity, oxidizing metal ions, NAD or NADP as acceptor; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
Gene3D; 2.30.110.10; -; 1.
InterPro; IPR002563; Flavin_Rdtase-like_dom.
InterPro; IPR012349; Split_barrel_FMN-bd.
Pfam; PF01613; Flavin_Reduct; 1.
SMART; SM00903; Flavin_Reduct; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Flavoprotein; FMN; NADP; Nucleotide-binding; Oxidoreductase;
Reference proteome.
CHAIN 1 169 Ferric-chelate reductase (NAD(P)H).
/FTId=PRO_0000430711.
NP_BIND 27 31 FMN. {ECO:0000244|PDB:1I0R,
ECO:0000244|PDB:1I0S,
ECO:0000269|PubMed:11525168}.
NP_BIND 45 52 FMN. {ECO:0000244|PDB:1I0R,
ECO:0000244|PDB:1I0S,
ECO:0000269|PubMed:11525168}.
NP_BIND 82 84 FMN. {ECO:0000244|PDB:1I0R,
ECO:0000244|PDB:1I0S,
ECO:0000269|PubMed:11525168}.
NP_BIND 147 154 NADP. {ECO:0000244|PDB:1I0S,
ECO:0000269|PubMed:11525168}.
BINDING 7 7 NADP. {ECO:0000244|PDB:1I0S,
ECO:0000269|PubMed:11525168}.
BINDING 89 89 FMN. {ECO:0000244|PDB:1I0R,
ECO:0000244|PDB:1I0S,
ECO:0000269|PubMed:11525168}.
BINDING 126 126 NADP. {ECO:0000244|PDB:1I0S,
ECO:0000269|PubMed:11525168}.
HELIX 3 8 {ECO:0000244|PDB:1I0R}.
STRAND 14 20 {ECO:0000244|PDB:1I0R}.
STRAND 23 30 {ECO:0000244|PDB:1I0R}.
STRAND 32 36 {ECO:0000244|PDB:1I0R}.
TURN 37 40 {ECO:0000244|PDB:1I0R}.
STRAND 41 47 {ECO:0000244|PDB:1I0R}.
HELIX 51 59 {ECO:0000244|PDB:1I0R}.
STRAND 60 68 {ECO:0000244|PDB:1I0R}.
HELIX 73 80 {ECO:0000244|PDB:1I0R}.
TURN 84 86 {ECO:0000244|PDB:1I0R}.
TURN 89 92 {ECO:0000244|PDB:1I0R}.
STRAND 95 97 {ECO:0000244|PDB:1I0R}.
STRAND 103 105 {ECO:0000244|PDB:1I0R}.
STRAND 109 122 {ECO:0000244|PDB:1I0R}.
STRAND 124 138 {ECO:0000244|PDB:1I0R}.
HELIX 147 154 {ECO:0000244|PDB:1I0R}.
STRAND 158 160 {ECO:0000244|PDB:1I0R}.
STRAND 165 167 {ECO:0000244|PDB:1I0R}.
SEQUENCE 169 AA; 18659 MW; D23950527048DEA9 CRC64;
MDVEAFYKIS YGLYIVTSES NGRKCGQIAN TVFQLTSKPV QIAVCLNKEN DTHNAVKESG
AFGVSVLELE TPMEFIGRFG FRKSSEFEKF DGVEYKTGKT GVPLVTQHAV AVIEAKVVKE
CDVGTHTLFV GEAVDAEVLK DAEVLTYADY HLMKKGKTPR TATVYFESK


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