ID   FERB_PARDE              Reviewed;          27 AA.
AC   P84469;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Ferric reductase B;
DE            EC=1.16.1.7;
DE   Flags: Fragment;
GN   Name=ferB;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, AND MASS SPECTROMETRY.
RX   PubMed=14728682; DOI=10.1046/j.1432-1033.2003.03957.x;
RA   Mazoch J., Tesarik R., Sedlacek V., Kucera I., Turanek J.;
RT   "Isolation and biochemical characterization of two soluble iron(III)
RT   reductases from Paracoccus denitrificans.";
RL   Eur. J. Biochem. 271:553-562(2004).
CC   -!- FUNCTION: Reductase activity that acts on Fe(3+)-chelates and uses both
CC       NADH and NADPH as electron donors. May play a role in iron uptake.
CC       {ECO:0000269|PubMed:14728682}.
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; EC=1.16.1.7;
CC         Evidence={ECO:0000269|PubMed:14728682};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:14728682};
CC       Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:14728682};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.4 mM for Fe(3+)EGTA and NADH {ECO:0000269|PubMed:14728682};
CC         KM=1.6 mM for Fe(3+)EDTA and NADH {ECO:0000269|PubMed:14728682};
CC         KM=0.4 mM for Fe(3+)citrate and NADH {ECO:0000269|PubMed:14728682};
CC         KM=0.4 mM for Fe(3+)chloride and NADH {ECO:0000269|PubMed:14728682};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14728682}.
CC   -!- INDUCTION: By Fe(3+) ion deprivation. {ECO:0000269|PubMed:14728682}.
CC   -!- MASS SPECTROMETRY: Mass=20196; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:14728682};
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DR   AlphaFoldDB; P84469; -.
DR   SMR; P84469; -.
DR   SABIO-RK; P84469; -.
DR   GO; GO:0140618; F:ferric-chelate reductase (NADH) activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; FAD; Flavoprotein; NAD;
KW   NADP; Oxidoreductase; Transport.
FT   CHAIN           1..>27
FT                   /note="Ferric reductase B"
FT                   /id="PRO_0000087228"
FT   NON_TER         27
FT                   /evidence="ECO:0000303|PubMed:14728682"
SQ   SEQUENCE   27 AA;  3012 MW;  10D878742BCD3F4B CRC64;
     MVKTVAVMVG SLRKDSLAHK LMKVLQK