YQJH_ECOLI
ID YQJH_ECOLI Reviewed; 254 AA.
AC Q46871; Q2M9D6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=NADPH-dependent ferric-chelate reductase;
DE EC=1.16.1.9;
DE AltName: Full=Ferric siderophore reductase;
GN Name=yqjH; OrderedLocusNames=b3070, JW3041;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18765906; DOI=10.1107/s174430910802352x;
RA Bamford V.A., Armour M., Mitchell S.A., Cartron M., Andrews S.C.,
RA Watson K.A.;
RT "Preliminary X-ray diffraction analysis of YqjH from Escherichia coli: a
RT putative cytoplasmic ferri-siderophore reductase.";
RL Acta Crystallogr. F 64:792-796(2008).
RN [4]
RP FUNCTION AS A FERRIC SIDEROPHORE REDUCTASE AND IN THE IRON HOMEOSTASIS,
RP CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21097627; DOI=10.1128/jb.01062-10;
RA Wang S., Wu Y., Outten F.W.;
RT "Fur and the novel regulator YqjI control transcription of the ferric
RT reductase gene yqjH in Escherichia coli.";
RL J. Bacteriol. 193:563-574(2011).
CC -!- FUNCTION: Plays a role in iron homeostasis under excess nickel
CC conditions. {ECO:0000269|PubMed:21097627}.
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; EC=1.16.1.9;
CC Evidence={ECO:0000269|PubMed:21097627};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33 uM for ferric ions (anaerobically at pH 7.5)
CC {ECO:0000269|PubMed:21097627};
CC KM=43 uM for NADPH (anaerobically at pH 7.5)
CC {ECO:0000269|PubMed:21097627};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Repressed by YqjI and Fur. YqjI is required for nickel-
CC dependent regulation of yqjH, while Fur is required for iron- and
CC cobalt-dependent regulation of yqjH. {ECO:0000269|PubMed:21097627}.
CC -!- DISRUPTION PHENOTYPE: Inactivation leads to ferrous iron chelator
CC resistance as the wild-type. {ECO:0000269|PubMed:21097627}.
CC -!- SIMILARITY: Belongs to the SIP oxidoreductase family. {ECO:0000305}.
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DR EMBL; U28379; AAA89149.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76105.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77120.1; -; Genomic_DNA.
DR PIR; C65095; C65095.
DR RefSeq; NP_417541.1; NC_000913.3.
DR RefSeq; WP_001066494.1; NZ_LN832404.1.
DR AlphaFoldDB; Q46871; -.
DR SMR; Q46871; -.
DR BioGRID; 4259593; 17.
DR BioGRID; 851898; 1.
DR IntAct; Q46871; 3.
DR STRING; 511145.b3070; -.
DR PaxDb; Q46871; -.
DR PRIDE; Q46871; -.
DR EnsemblBacteria; AAC76105; AAC76105; b3070.
DR EnsemblBacteria; BAE77120; BAE77120; BAE77120.
DR GeneID; 947582; -.
DR KEGG; ecj:JW3041; -.
DR KEGG; eco:b3070; -.
DR PATRIC; fig|511145.12.peg.3164; -.
DR EchoBASE; EB2787; -.
DR eggNOG; COG2375; Bacteria.
DR HOGENOM; CLU_040923_4_0_6; -.
DR InParanoid; Q46871; -.
DR OMA; VHAFVHG; -.
DR PhylomeDB; Q46871; -.
DR BioCyc; EcoCyc:G7593-MON; -.
DR BioCyc; MetaCyc:G7593-MON; -.
DR SABIO-RK; Q46871; -.
DR PRO; PR:Q46871; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IBA:GO_Central.
DR GO; GO:0071289; P:cellular response to nickel ion; IMP:EcoCyc.
DR GO; GO:0033212; P:iron import into cell; IBA:GO_Central.
DR GO; GO:0015891; P:siderophore transport; IBA:GO_Central.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IMP:EcoCyc.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR013113; FAD-bd_9_SIP.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR007037; SIP_C.
DR InterPro; IPR039374; SIP_fam.
DR PANTHER; PTHR30157; PTHR30157; 1.
DR Pfam; PF08021; FAD_binding_9; 1.
DR Pfam; PF04954; SIP; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..254
FT /note="NADPH-dependent ferric-chelate reductase"
FT /id="PRO_0000169437"
FT DOMAIN 15..136
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
SQ 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
