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Database: UniProt
Entry: A4HMS7_LEIBR
LinkDB: A4HMS7_LEIBR
Original site: A4HMS7_LEIBR 
ID   A4HMS7_LEIBR            Unreviewed;       832 AA.
AC   A4HMS7;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 2.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=NADPH--hemoprotein reductase {ECO:0000256|ARBA:ARBA00023797};
DE            EC=1.6.2.4 {ECO:0000256|ARBA:ARBA00023797};
GN   ORFNames=LBRM_34_2490 {ECO:0000313|EMBL:CAM43466.2};
OS   Leishmania braziliensis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC   Leishmania braziliensis species complex.
OX   NCBI_TaxID=5660 {ECO:0000313|EMBL:CAM43466.2, ECO:0000313|Proteomes:UP000007258};
RN   [1] {ECO:0000313|EMBL:CAM43466.2, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM43466.2,
RC   ECO:0000313|Proteomes:UP000007258};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM43466.2, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM43466.2,
RC   ECO:0000313|Proteomes:UP000007258};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; FR799009; CAM43466.2; -; Genomic_DNA.
DR   RefSeq; XP_001568357.2; XM_001568307.2.
DR   AlphaFoldDB; A4HMS7; -.
DR   STRING; 5660.A4HMS7; -.
DR   GeneID; 5419309; -.
DR   KEGG; lbz:LBRM_34_2490; -.
DR   VEuPathDB; TriTrypDB:LbrM.34.2490; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_340032600; -.
DR   InParanoid; A4HMS7; -.
DR   Proteomes; UP000007258; Chromosome 35.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   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; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
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   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007258}.
FT   DOMAIN          79..285
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          394..636
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   832 AA;  91288 MW;  D6A53B9338A8E660 CRC64;
     MVQKRYLALV GLLVLGATSS VLLRRQRKVQ RERREFAERY VKQIKAAREA HAQCLNGGSA
     SQDSGDISDA DLDDESATVK VIYGSESGNA EALAKGFVMT LRDRGVQAAL IDPSRWSYME
     DYLYHNKRNV PLFHPIKVTS PNSHTAKKKL CKTPEKAKES SPPLVYIFIV ATAGEGDPTG
     NFMALFHEMQ AAVRRATTDK VSTQSSDAAA PAAPFSATAE APFKNIYYAV FGLGDSSYKY
     YCRSATDTNT LLKKGGGISV HRVGFGDARN GMQEDVFDEW QEKVMLALEE KCGLEMTTGT
     RAPPKPELQF RFLSSAAATT AATTSTTPQA CPCGATAATA APSAPVVTDN AAPNHRALSS
     TAIPSSSVEA ESTSAPPLSL PFPPPPMLLE PSLMNPTRIR LVTKTQLTQP RDSDGSSVYC
     FCFESEGTGI SYQAGDHLGI FPTSPPDMVA RYAKALSIPA DELETSVELC ETVPSRGILR
     NVLPACVPLR VVLQRYVDLC GRPKKSTLRV LAKYCTDLVQ KEAFLDLLRL PAEKEVEETG
     ARTSSARKPK KLRTVVDYLE KFPSCCCIPL GHFIEIMPRT QPRYYSIASD RMSHGTKVEI
     IVRVLTDGLA SSYLAHRVEE GEEVFAYVCI SAFHLPQRIG ENRPILMIGP GTGAAAMVGL
     CYKKEALMRK QPAAQYGPTV FLFGAQYRQT EYFVEEELQR WSMAPAEMRQ WDINHPTSHA
     GLAARRSKTH STEPLSNSVI TMVDCAFSRD QAEKIYVTSL IDKHKDLLYG MLTSTSGGGC
     LIFLSGDASC MAKDVDRALV ALLQDRGGMT RMAAIEYLRR MESDHRYLKD VY
//
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