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Database: UniProt
Entry: K2SBK4_MACPH
LinkDB: K2SBK4_MACPH
Original site: K2SBK4_MACPH 
ID   K2SBK4_MACPH            Unreviewed;       834 AA.
AC   K2SBK4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Nitrate reductase [NADPH] {ECO:0000256|ARBA:ARBA00015499};
DE            EC=1.7.1.3 {ECO:0000256|ARBA:ARBA00012673};
DE   Flags: Fragment;
GN   ORFNames=MPH_08578 {ECO:0000313|EMBL:EKG14250.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG14250.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG14250.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG14250.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
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=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000256|ARBA:ARBA00001924};
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:EKG14250.1}.
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DR   EMBL; AHHD01000363; EKG14250.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2SBK4; -.
DR   STRING; 1126212.K2SBK4; -.
DR   VEuPathDB; FungiDB:MPH_08578; -.
DR   eggNOG; KOG0535; Eukaryota.
DR   eggNOG; KOG0537; Eukaryota.
DR   HOGENOM; CLU_003827_4_2_1; -.
DR   InParanoid; K2SBK4; -.
DR   OrthoDB; 1239at2759; -.
DR   Proteomes; UP000007129; Unassembled WGS sequence.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.40.650; -; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 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; IPR014756; Ig_E-set.
DR   InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR   InterPro; IPR008335; Mopterin_OxRdtase_euk.
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; PF00174; Oxidored_molyb; 1.
DR   PRINTS; PR00407; EUMOPTERIN.
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; SSF56524; Oxidoreductase molybdopterin-binding domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT   DOMAIN          670..748
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   REGION          118..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         834
FT                   /evidence="ECO:0000313|EMBL:EKG14250.1"
SQ   SEQUENCE   834 AA;  95094 MW;  54D3F573BB32B4A5 CRC64;
     MPPVLWTVKV QNHPGSSADD IAKEPDWGAG LRHRIGFKND QDRVPGITHL EDEYDEDVEE
     AREELVELNT RSEGPQLINF RDAMGNQKDL HRWTNESRSI GWRYVLEASE HWIKNTEDWP
     ANAKKRQQAK NQRMKEEDRG GQQEHEWKRS QGENKHHNAY AGVEESGYDS GIEQSGQAGN
     QESDQGKLRK KYSPQEITLL RSLRHEKEYI SQLKCNNGKR RSPQQHNKTP IFINEQDQCS
     PDNWLPRSSD LIRLTGKHPL NAEAPLSHLF DAGLITPNEL HYVRNHGAVP RLLWELHKLD
     IQGGHMTLSM DDLKDKFATI NIPIALACDG NRRKELHMIK KSKGFSWGAG AVGCAYWKGP
     LLRDVLLSAG IPEIMPGGDG KRYWVHFEGA DEPSEAKYAT CLPFQYVMDP TNDVILAYEM
     NDLPLPPDHG YPVRLMVPGY VGGRCVKWLK KIWISDKEND SHHHVWDNRL LPSFVTEKDG
     EFAEAMFRHP DTACNEQNLN SVIVKPAHGE RIPLTTARKG HSYRIAGYAY DGGGHEVQRV
     EVSLDDGETW LYCIRQFPDY PIRHGNKFWT WLHWHVDVEL SHLLRSKSIT VRCFNVFKNT
     QPEKPSWNIM GVMNNCWYVV KPSIVDGEET DVPSILFEHP VEPGTGAGGW MKPSTESRIE
     NAKQEAGTPQ KQFTRQEIEK HDKEDDCWIV IDGKVYDATS LLSWHPGGKA AVLGHAGKLH
     QETSDEFASI HDGYAYQKLK ECVLGIVTEK AADFIKKNDE AAAKDEASSQ DNDDQLTLQK
     HRWLPVRLID REDISKDTRT YTFALPDGKS VLGLGTCQHV QIGFHMKDRM LIRS
//
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