ID A0A0J8RCC0_COCIT Unreviewed; 1078 AA.
AC A0A0J8RCC0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=CISG_09600 {ECO:0000313|EMBL:KMU82070.1};
OS Coccidioides immitis RMSCC 3703.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU82070.1, ECO:0000313|Proteomes:UP000054559};
RN [1] {ECO:0000313|Proteomes:UP000054559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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:0000256|ARBA:ARBA00000496};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000256|ARBA:ARBA00006278}.
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DR EMBL; DS268214; KMU82070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8RCC0; -.
DR STRING; 454286.A0A0J8RCC0; -.
DR Proteomes; UP000054559; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IEA:UniProt.
DR GO; GO:0006826; P:iron ion transport; IEA:UniProt.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 2.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR32361:SF23; FERRIC-CHELATE REDUCTASE-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054559};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT TRANSMEM 400..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 554..572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 592..610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 630..651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 658..678
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 690..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 717..828
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1078 AA; 122544 MW; 998428A5BBAFC392 CRC64;
MGDVHSGFCS VGTTRLKIRG NWGVTRLNAL STLGSYGVRG RVPVESPMMM RIQTSQWSTS
DSIPWDSNVT LDKIGEHDDR LSLDCRGNEE QDRAPCSVLL YAAGWLVYAT FLSPTLHPVN
FLALHSLAPC LRRSNGILFP VQYLLTEVSR STRWVECLPR TWIPSELFEA FRGLSDTKKL
HHQLQASLGG EKIFQSVFGV ELRSSPCGWD TLDSRPVLPP HRDFRSHYQG NVHHFFFVST
EICSHSLHRQ SRHNFAHPQI FLATLAIDLA HLNIVKYHCT HPSAAFLRPL LSGSSQPKDT
FTSIDSISGS RFNETSDYRQ KARILYFSER STKPNRFFPI SIMMSPLNGW KVLSPGWVSR
DTQGSLVSIV KRIDIPITSM TTPGQLEASR HDPFNQASKY ALGWVYFSIV LLVFTFVIRS
YHIWGDKIRA ALYREELRNF DKSLELDHEM ATPATANSTS SFFPVHGALP PPPKRESAIA
SMRWLNYSIA FVRWIFYRPI PVIRLWKLEI VPPSLGAIFI VGLAFIFVTL YSFVPQPLFY
NSIRDGSPPL AIRAGMLSVS LLPWIIALSM KANLISMLTG IGHERLNVLH RWAGYLCMFL
ALVHMIPFFI TPVWEDGALE LFRQFIKGDY YIYGSGLAAL VPLAVLCLHS LPIFRNRMYE
LFVTLHAPIS VVFVGMMFWH CANFLTSWHY LYTTVAIWAA SYIIRVFYLN WTNPFRLSWL
IGEESAVTIL PENAVKVTIP TQMRWRPGQY VYLRMPGISI FENHPFTIAS LCSDEFPSSY
GEEYRDMALV FRPFGGFTNK VLNTALVKGP FKTYRAFIDG PYGGMRRELA AFDHVVFFAG
GSGITAIASQ LLDLIKRMRD GKALTRTESS YLREYAPPGT VSFHFYLTGS TRYTHQPSRS
RPHSGAFHDK INDVFQGVAS KRDSAYIREE AAGDEEREKE LRRENEDTIA ALPSAYIPPK
QSYGWNFPAS PPPEQDPSSS SMNFGFPSTP TMLQKNLMRF AFLPTQKRDG WKTEYGRPDI
PFMLRQYSKD FGRRSCVFVC GPPSMRVDVA NTVARLQRKI MDDPNKTELF LHAENYAI
//
