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NADPH-dependent ferric-chelate reductase (EC 1.16.1.9) (Ferric siderophore reductase)

 YQJH_ECOLI              Reviewed;         254 AA.
Q46871; Q2M9D6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-OCT-2018, entry version 115.
RecName: Full=NADPH-dependent ferric-chelate reductase;
EC=1.16.1.9;
AltName: Full=Ferric siderophore reductase;
Name=yqjH; OrderedLocusNames=b3070, JW3041;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[3]
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=18765906; DOI=10.1107/S174430910802352X;
Bamford V.A., Armour M., Mitchell S.A., Cartron M., Andrews S.C.,
Watson K.A.;
"Preliminary X-ray diffraction analysis of YqjH from Escherichia coli:
a putative cytoplasmic ferri-siderophore reductase.";
Acta Crystallogr. F 64:792-796(2008).
[4]
FUNCTION AS A FERRIC SIDEROPHORE REDUCTASE AND IN THE IRON
HOMEOSTASIS, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE,
BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=21097627; DOI=10.1128/JB.01062-10;
Wang S., Wu Y., Outten F.W.;
"Fur and the novel regulator YqjI control transcription of the ferric
reductase gene yqjH in Escherichia coli.";
J. Bacteriol. 193:563-574(2011).
-!- FUNCTION: Plays a role in iron homeostasis under excess nickel
conditions. {ECO:0000269|PubMed:21097627}.
-!- CATALYTIC ACTIVITY: 2 Fe(II)-siderophore + NADP(+) + H(+) = 2
Fe(III)-siderophore + NADPH. {ECO:0000269|PubMed:21097627}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=33 uM for ferric ions (anaerobically at pH 7.5)
{ECO:0000269|PubMed:21097627};
KM=43 uM for NADPH (anaerobically at pH 7.5)
{ECO:0000269|PubMed:21097627};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- INDUCTION: Repressed by YqjI and Fur. YqjI is required for nickel-
dependent regulation of yqjH, while Fur is required for iron- and
cobalt-dependent regulation of yqjH.
{ECO:0000269|PubMed:21097627}.
-!- DISRUPTION PHENOTYPE: Inactivation leads to ferrous iron chelator
resistance as the wild-type. {ECO:0000269|PubMed:21097627}.
-!- SIMILARITY: Belongs to the SIP oxidoreductase family.
{ECO:0000305}.
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EMBL; U28379; AAA89149.1; -; Genomic_DNA.
EMBL; U00096; AAC76105.1; -; Genomic_DNA.
EMBL; AP009048; BAE77120.1; -; Genomic_DNA.
PIR; C65095; C65095.
RefSeq; NP_417541.1; NC_000913.3.
RefSeq; WP_001066494.1; NZ_LN832404.1.
ProteinModelPortal; Q46871; -.
SMR; Q46871; -.
BioGrid; 4259593; 17.
IntAct; Q46871; 3.
STRING; 316385.ECDH10B_3245; -.
EPD; Q46871; -.
PaxDb; Q46871; -.
PRIDE; Q46871; -.
EnsemblBacteria; AAC76105; AAC76105; b3070.
EnsemblBacteria; BAE77120; BAE77120; BAE77120.
GeneID; 947582; -.
KEGG; ecj:JW3041; -.
KEGG; eco:b3070; -.
PATRIC; fig|511145.12.peg.3164; -.
EchoBASE; EB2787; -.
EcoGene; EG12953; yqjH.
eggNOG; ENOG4105Q26; Bacteria.
eggNOG; COG2375; LUCA.
HOGENOM; HOG000221089; -.
InParanoid; Q46871; -.
KO; K07229; -.
OMA; VPDIFDS; -.
PhylomeDB; Q46871; -.
BioCyc; EcoCyc:G7593-MONOMER; -.
BioCyc; MetaCyc:G7593-MONOMER; -.
PRO; PR:Q46871; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IDA:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
GO; GO:0071289; P:cellular response to nickel ion; IMP:EcoCyc.
GO; GO:0033212; P:iron assimilation; IMP:EcoCyc.
Gene3D; 3.40.50.80; -; 1.
InterPro; IPR013113; FAD-bd_9_SIP.
InterPro; IPR017927; FAD-bd_FR_type.
InterPro; IPR039261; FNR_nucleotide-bd.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
InterPro; IPR007037; SIP_C.
InterPro; IPR039374; SIP_fam.
PANTHER; PTHR30157; PTHR30157; 1.
Pfam; PF08021; FAD_binding_9; 1.
Pfam; PF04954; SIP; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase;
Reference proteome.
CHAIN 1 254 NADPH-dependent ferric-chelate reductase.
/FTId=PRO_0000169437.
DOMAIN 15 136 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
SEQUENCE 254 AA; 28872 MW; 889F25AF95B78DBD CRC64;
MNNTPRYPQR VRNDLRFREL TVLRVERISA GFQRIVLGGE ALDGFTSRGF DDHSKLFFPQ
PDAHFVPPTV TEEGIVWPEG PRPPSRDYTP LYDELRHELA IDFFIHDGGV ASGWAMQAQP
GDKLTVAGPR GSLVVPEDYA YQLYVCDESG MPALRRRLET LSKLAVKPQV SALVSVRDNA
CQDYLAHLDG FNIEWLAHDE QAVDARLAQM QIPADDYFIW ITGEGKVVKN LSRRFEAEQY
DPQRVRAAAY WHAK


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