ID A0A421JMY9_9ASCO Unreviewed; 1387 AA.
AC A0A421JMY9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN ORFNames=JA1_003314 {ECO:0000313|EMBL:RLV92257.1};
OS Spathaspora sp. JA1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV92257.1, ECO:0000313|Proteomes:UP000285775};
RN [1] {ECO:0000313|EMBL:RLV92257.1, ECO:0000313|Proteomes:UP000285775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA1 {ECO:0000313|EMBL:RLV92257.1,
RC ECO:0000313|Proteomes:UP000285775};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV92257.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NSGQ01000026; RLV92257.1; -; Genomic_DNA.
DR STRING; 2028339.A0A421JMY9; -.
DR Proteomes; UP000285775; 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; 2.
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:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR Pfam; PF08022; FAD_binding_8; 2.
DR Pfam; PF01794; Ferric_reduct; 2.
DR Pfam; PF08030; NAD_binding_6; 2.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 2.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 2.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 2.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 2.
DR PROSITE; PS51384; FAD_FR; 2.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000285775};
KW Signal {ECO:0000256|SAM:SignalP};
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:ARBA00022448}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1387
FT /note="ferric-chelate reductase (NADPH)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019489339"
FT TRANSMEM 156..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..854
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 905..927
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 948..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 995..1011
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1023..1045
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1052..1069
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 407..526
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 1086..1205
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1387 AA; 159650 MW; 187575EDD303A8AA CRC64;
MNLLNSLYLL IFFIIGAKAS APGIDWYTPY LGLYACLYEV DYSGNFTFCP ANDTTCLCSN
ENSRATMAGC LVYQSRNTTT MIDYIVNYCS MYFSTDLKPT WFEEAIELYE KKAKYLTDIE
LPADNIVDIP LKFEPKDMDY FAQVALLFLG NYDDSVWYGV SVYGFWFLVL LVGTISHWTK
MLFPSFTKKL TGPVSNFYRK HISMPALYGR RKAQSLPGFK VFDSLIPARF EMIVIALFYI
FMIVVHTINM KGVKDDPVFG STYLAELRYV ADRTGIVGTA IMPLVFLFAG RNNFLQWICG
FNYQTFLCYH RHLARVMFML IVIHSVNFTI LEKDYFASDM QQTYFYWGVI ATIVGGLMLI
QSILFLRRIN YELFLIVHIV LAAFWVAGSW VHMVDFGYGC IFFPAIAVWC FDRLVRLVRL
FYFGFPEVNL QLVADETIKL TIPKPKHWPI IPGGHAFIYF MKPRYFWQSH PFTFTSSVQE
DNNIVMYIKL KGGVTHSLYK LLNKSPGKTV NMRVGVEGPY GESTPAKYAD KAVFIAGGNG
IPGIYSEISD IASRSSKERK SVLKLIWVIR EYKSLVWFHE ELMKLKDTNI DTTVYVTRPN
VKLSNIEELK NSESSKEGSI EEITKSTSFE SEDFVEQLKD ELSHIHFEEG RPNIEQFIQE
EIKESPGSIA FVACGHPKMV DEVLYLFYLL FLFANGTNAD EKLQWYKKHI GLYSCLYPIF
YLEGAAFCPD MDETCICSND NSRATIAGCL AYKDRVTSAN INFFIQYCEM YYETSLDEDW
YDKSLARFND KAKFLSEIDL PADNIPHVPL RFESKDMDYY AKVAINFLGN YDDSIWYGVS
VFGFWLIVLI IGAVRHWSKV LFPEISKNLN GPISNFYRKY ISTPALYGRR KTQSLPGFKV
FDSLIPARIE MIVIALFYIF ITIINAVNIQ AVKGDPIWGS KYMAEIRYVA DRTGIIGTVM
MPLVFLFSGR NNFLQWFCGI NSATSLCYHR HTARVMFILI AIHSVTYTIN YGSEYVEELE
DPWLYWGLIA TIIGGLMLIQ SILFLRRNYY EVFLVVHIVM AVLYVVGTWI HIVDLGYGCI
LYPSIAVWCF DRLIRLVRLF YFGFPEVTLK LVADETIKLT IPKPKHWPII PGGHAFIYFM
KPKYFWQSHP FTFTSSVQED NNIVMYIKLK GGITHRLYKL LNKSPGKTVN MRVGVEGPYG
ESTPAKYADK AVFIAGGNGI PGIYSEVSDI ALRSSKERKS VLKLIWVIRE YKSLTWFHEE
LLKLKETNID TTIYVTRPDV KLSNVEDLKN SESSKEGSIE LTKSTSFESD DFVEQLKDEL
SHIHFEEGRP NIEQLLQEEI KESPGSIAFV TCGHPIMVDE IRYYCCKNIG NPEKKRIDFY
EQLQVTH
//
