ID R9P930_PSEHS Unreviewed; 1618 AA.
AC R9P930;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 22-FEB-2023, entry version 49.
DE RecName: Full=NADPH-dependent diflavin oxidoreductase 1 {ECO:0000256|HAMAP-Rule:MF_03178};
DE EC=1.18.1.- {ECO:0000256|HAMAP-Rule:MF_03178};
DE AltName: Full=NADPH-dependent FMN and FAD-containing oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03178};
GN Name=TAH18 {ECO:0000256|HAMAP-Rule:MF_03178};
GN ORFNames=PHSY_005449 {ECO:0000313|EMBL:GAC97861.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC97861.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
CC -!- FUNCTION: NADPH-dependent reductase which is a central component of the
CC cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery.
CC Transfers electrons from NADPH via its FAD and FMN prosthetic groups to
CC the [2Fe-2S] cluster of DRE2, another key component of the CIA
CC machinery. In turn, this reduced cluster provides electrons for
CC assembly of cytosolic iron-sulfur cluster proteins. Positively controls
CC H(2)O(2)-induced cell death. {ECO:0000256|HAMAP-Rule:MF_03178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [2Fe-2S]-[protein] = H(+) + NADP(+) + 2
CC reduced [2Fe-2S]-[protein]; Xref=Rhea:RHEA:67716, Rhea:RHEA-
CC COMP:17327, Rhea:RHEA-COMP:17328, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000256|HAMAP-Rule:MF_03178};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_03178};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|HAMAP-Rule:MF_03178};
CC -!- SUBUNIT: Interacts with DRE2; as part of the cytosolic iron-sulfur (Fe-
CC S) protein assembly (CIA) machinery. {ECO:0000256|HAMAP-Rule:MF_03178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03178}.
CC Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03178}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Note=Relocalizes to mitochondria after
CC H(2)O(2) exposure. {ECO:0000256|HAMAP-Rule:MF_03178}.
CC -!- SIMILARITY: Belongs to the NADPH-dependent diflavin oxidoreductase
CC NDOR1 family. {ECO:0000256|HAMAP-Rule:MF_03178}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000256|HAMAP-
CC Rule:MF_03178}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC family. {ECO:0000256|HAMAP-Rule:MF_03178}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03178}.
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DR EMBL; DF238814; GAC97861.1; -; Genomic_DNA.
DR RefSeq; XP_012191448.1; XM_012336058.1.
DR STRING; 1305764.R9P930; -.
DR GeneID; 24110727; -.
DR eggNOG; KOG1159; Eukaryota.
DR HOGENOM; CLU_245674_0_0_1; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000014071; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:InterPro.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.5.1500; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_03178; NDOR1; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR028879; NDOR1.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR013907; Sds3.
DR PANTHER; PTHR19384:SF10; NADPH-DEPENDENT DIFLAVIN OXIDOREDUCTASE 1; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF08598; Sds3; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM01401; Sds3; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03178};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_03178};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_03178};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_03178};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03178};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03178};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03178}; Reference proteome {ECO:0000313|Proteomes:UP000014071};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 981..1125
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1175..1463
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..53
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..184
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..245
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..803
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 987..992
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 1034..1037
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 1072..1081
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 1107
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 1357
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 1387..1390
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 1434..1437
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 1474
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 1533..1534
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 1540..1544
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
FT BINDING 1617
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03178"
SQ SEQUENCE 1618 AA; 176447 MW; 9B88058A22E741BD CRC64;
MPSSAASQSN TAAAHSSAAA TKHTHLDIAD SSDAETEPLP YDDDDDQDAP ADDVMDLDQL
AQHAAASAAL PTDQDAPGEP ADVSMDPSND SQLEPSQAED LADLPASQLT ATHDPNSNMS
SPQKTGGFTG DEFSDESELT DEDDEQNQDE DASSLSDDDL GGSDDEDEDD EDEEDEDQDD
EDTASKTHED EAAEALAALT GGADDENDNA GAAAGLDALA ALATAGDADD DQDDQDDDDV
SDPEDGETAT ASAAIGGAAK PVRVSLLRQS GGDDDGLSSD ITPEPEDADA AADDASDHPG
SPRDTDLDLI ASMKKRAAAT GGATSLLEPE QLVDSLPGSA SSSRAASPLA DEDDDAEKPK
QADDADAEID AKHAQADQAD AEHPDTAVGT PAPDAAEQDD DTSTDEAAIR RQEAMEALTK
IEIGFAMLRD RLYVERLQEI SKEGDMILEG THPELLHLTK AIETRRERRT ELVDMWFEHQ
EKQYERVAKA EEFAAWSIWR SSCAGLRRDM MDEYSRKRRR LDREKRTLDA PRPARRHQIF
ETELVRNPDR LHIPLTSFSL PEDAEPTRAS GSKIGRKQSA KRKALAREIE AGDEFVAYPD
LKGLAEADVM MDIEQMGIRP AGMPPGMYDP FYGAPVGLEF QNPEVYAMYG PEAAAAAAAA
AAQAHMNGVP YNLPPGARGL PPPPPGAMMA PGTPGSIHTP HRHGHALPPP PPGHMHPGMD
MGMMPFDPYA AAEMERAARM HHREQQARMG IDLNDPHHRS SPFPPDMYQP YPPHFNMPPG
AGGPGPGMRP GMSNMPPSPT PPHRASSGGR KERASMEDGV HVSGRGRGAA KTPGRSKQPR
SSQPRDGHVG GGGVVESPTQ AKSTGGAKPN LPPPPSMPVG AVGAMDERDH KVIRAREAHE
SSRVVSTLCK MYREFDRREV DRVIRNSFLL CRFATFAVRP SSPSILLLFL PSKLLAKMTS
IRASTSSSAS NESGPSQPRH LTILYMTQTG TSSDLALRIS RQAQRKRFST TVCDVSSYDP
ADLVSENYVL FLVSTTGQGE FPTSSRGFWN FLLRKGIPED ILEDVRFAAF GLGDSTYPRF
CWPVRLLSRR LKGLGAVEVV EHGEGDEMHY LGLEGELKPW LEEFWGKMDE LCPLEEGERE
VGRDELLPPA VTIRKVDGEE EGGGTYGFDE HLLEQGWSMS RLGKNDRMTA ADHFQDVRLL
EFVESPSSAG AVQNGENGEA STKSAAASDD VNFQSYRPGD VLCLHPINDA LSVTEFLDRL
KLDPDTLITL SGSTVPTTAP QSPHPISVRD LFTYHLDFTS VPTHSFFEQI RLFSPTGSLE
REKLDEYCGI LPEDELAKGA NPQDGIDEMY EYAQRPRRTI KEVLEEFKSV GIPLEYVADV
IPWIKPREFS IASAPPTASL SRGSKGDASD QPHAIQLSVA IVKYKTRLRK SRTGLCTRWL
STLPVDAEVP IWIKPGYLTL PPPDAPLILI GPGTGCAPLR SLVIQRLSSP NPAREIHLFL
GFRYRAKDFL FQNDWQALQQ HHANHFHLHT AFSRDGGDEK TYVQDLIVKE ENRGMLWEAI
TETNAWIVVA GASGKMPEQV RGAFERVARE EGGMDEDQAK RFLDGLERQR RWQEECWS
//
