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Database: UniProt
Entry: F0UMG9_AJEC8
LinkDB: F0UMG9_AJEC8
Original site: F0UMG9_AJEC8 
ID   F0UMG9_AJEC8            Unreviewed;       855 AA.
AC   F0UMG9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Nitrate reductase [NADPH] {ECO:0000256|ARBA:ARBA00015499};
DE            EC=1.7.1.3 {ECO:0000256|ARBA:ARBA00012673};
GN   ORFNames=HCEG_06528 {ECO:0000313|EMBL:EGC47313.1};
OS   Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN   [1] {ECO:0000313|Proteomes:UP000008142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC       of nitrate assimilation in plants, fungi and bacteria.
CC       {ECO:0000256|ARBA:ARBA00003838}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NADP(+) + nitrite = H(+) + NADPH + nitrate;
CC         Xref=Rhea:RHEA:19061, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.7.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000195};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000256|ARBA:ARBA00001924};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the nitrate reductase family.
CC       {ECO:0000256|ARBA:ARBA00006253}.
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DR   EMBL; DS990640; EGC47313.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0UMG9; -.
DR   STRING; 544711.F0UMG9; -.
DR   VEuPathDB; FungiDB:I7I53_00764; -.
DR   HOGENOM; CLU_003827_4_0_1; -.
DR   OMA; KAMMPDY; -.
DR   Proteomes; UP000008142; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   CDD; cd06183; cyt_b5_reduct_like; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 3.90.420.10; Oxidoreductase, molybdopterin-binding domain; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR   InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR   InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19372:SF7; SULFITE OXIDASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR19372; SULFITE REDUCTASE; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF03404; Mo-co_dimer; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF00174; Oxidored_molyb; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   PRINTS; PR00407; EUMOPTERIN.
DR   PRINTS; PR00371; FPNCR.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF56524; Oxidoreductase molybdopterin-binding domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008142}.
FT   DOMAIN          495..570
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          597..709
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   855 AA;  95077 MW;  BE00DF3C02D4EFD7 CRC64;
     MAAAELGEST VALSLAANPD KLRVALRAPA TAHSTLFCRT ARRLRGSLIG FTYGRWIFIL
     LMPIPLVSEI IPVNRNIYEF NIKMESIMRL EDFPTVLIQK KSLVPHISQQ PAHAEKGAPR
     AAYIPLPPPS KEPTEILDID KDTPDKHVPR DPRLIRLTGI HPFNVEPPLT SLYDEGFLTS
     PELFYVRNHG SVPEVRQADI PDWQLSVEGL VQSPLVLNLA QILTEFEQIT APITLVCAGN
     RRKEQNQVRK SKGFSWGAAG VSTALFTGPL MSSILQRAKL LPGAKYVCME GADKLPNGCY
     GTSIKLNWAM DPNKRIMLAH KMNGEPLRPD HGRPLRAVVP GQIAWRLANI EYPEDKYREV
     DQNLYGGKID MSWQETCFCW CFWSLKISTT ELEGSDGILV RAMDEAMNIQ PRNMYWSVLG
     MMNNPWFCVA ITKQDGYLRF EHPTQPALIP GGWMERVKRN GGDLVNGNWG AMVEGCEKPA
     VMEGPKIDLK KPGLNITISL ENFRRHQIGP QPWFALEGEV YDGTAFLNEH PGGAQSILSA
     AGLDITEEFM AIHSETAKVM MSDYHIGSLD LSSQETLKND TNESALSPSR EVFLNSKFWA
     PSSLRSKTVV SPDSRLFTFR LSHGSQFLGL PVGNHVMLKI DDPSTGETII RAYTPISKQD
     SRGTIDILVK LYPSTPNHPN GGKMTTAMDK LPLGAVVKFK GPIGKFEYLG NGEVLLNEKK
     RYVQSFHMIC AGSGITPIFQ ILRAVIEDPE DRTSCVVLDG NRTEADILCR AELDDFMTEN
     SNGKCRIVHT LTQPSSVWTG RKGRISEDLL LEYVPVNAKG NVNSLVLVCG PEALEVAVRN
     TLLSMGWNEC DLIFF
//
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