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Database: UniProt
Entry: A0A1Y2NAA8_PSEAH
LinkDB: A0A1Y2NAA8_PSEAH
Original site: A0A1Y2NAA8_PSEAH 
ID   A0A1Y2NAA8_PSEAH        Unreviewed;      1396 AA.
AC   A0A1Y2NAA8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=NADH oxidase {ECO:0000313|EMBL:OSY44099.1};
DE            EC=1.-.-.- {ECO:0000313|EMBL:OSY44099.1};
GN   ORFNames=BG845_00220 {ECO:0000313|EMBL:OSY44099.1};
OS   Pseudonocardia autotrophica (Amycolata autotrophica) (Nocardia
OS   autotrophica).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=2074 {ECO:0000313|EMBL:OSY44099.1, ECO:0000313|Proteomes:UP000194360};
RN   [1] {ECO:0000313|EMBL:OSY44099.1, ECO:0000313|Proteomes:UP000194360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 535 {ECO:0000313|EMBL:OSY44099.1,
RC   ECO:0000313|Proteomes:UP000194360};
RA   Grumaz C., Vainshtein Y., Kirstahler P., Sohn K.;
RT   "Pseudonocardia autotrophica DSM535, a candidate organism with high
RT   potential of specific P450 cytochromes.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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:OSY44099.1}.
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DR   EMBL; MIGB01000001; OSY44099.1; -; Genomic_DNA.
DR   STRING; 2074.BG845_00220; -.
DR   Proteomes; UP000194360; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR023967; CHP03996_oxidoreductase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   NCBIfam; TIGR03996; mycofact_OYE_1; 1.
DR   PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR   PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR   Pfam; PF12831; FAD_oxidored; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   Pfam; PF00724; Oxidored_FMN; 2.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 2.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:OSY44099.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194360}.
FT   DOMAIN          4..313
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          730..1060
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   REGION          332..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          703..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1396 AA;  143082 MW;  217B9E628C7C6259 CRC64;
     MLFGPHETNL GSGARGISDD HVAYYAERAA GGAGLVVVEP ASVHPSDHPY AYAPAASGPT
     ARGWAAVAEA CRAHGTLVLA GLAHAGGQGS TAHSGHPLWG PSAVPDVVSR EVPVAMDAAQ
     IGELVLGFTT AARSAVDNGV DGVEISAGQH SVLRQFCSGL TNHRADAYGR DRSLLLRQVL
     AAVRAEIGPE PLLSLRLCVD ELAPWAGITP DDGMALARAV ADDVDLLVPV VGSGLSVAAT
     RPDLHTPEAF LRERCGAVRR AVRGAALVVL AGSVAAPGIA EEALACGDAD IVEMTRAQIA
     DPALVALVRA GTPERVRPCL LSNALAAARD PRNPVVGDEL EPRSGHERTE PSVAGGPAPG
     AAPARTGDRP ERVPVLVVGG GPAGLEAART LALLGHPVAL HERSSRLGGM LHAAAALPGR
     DRMALPVAWW EREIRRLGVL IELGSELDAT ALAAAEARGE AVLLATGSGP APSGIEADVP
     VLPVAELVHP DRGGVAVLAA AGIPDGAPVL VRDPIGDWSG PGAAELLVAA GYRVTLATPD
     AVAGHQLGRC GDMAPANARL ERAGVVRALF SAVRRVRDGR AELVDVHTGA RTTVECAVVV
     DCAARLPDRT IPDGPDRWSA GDRVAPRTLA EAVREGRRAA MALGGRRGVG SADGERRRIA
     LVPPAPGRAA APAGECTLGT SLGTVQAGAG YAAVPGPVAY PGNRSAPVSG SGPRRAARPP
     DRASPARLGD PLRLGRHELR NRIVFTAHLT GFAEDGLPTP RHTAYYAARA AGGAGLVITE
     EHAVHPGDRP YERLIRGHDP AVLPAYRALT DAVHAHGAVV LAQLNHNGAQ GSGMYSREPV
     VGPSALPDPM FREVPAELDA AGIAEIVAAF ADVAARCVDG GFDGVELQCS HASLLRLFLS
     PATNRRTDAW GRDRAKIVLD VVAAVRAAIG PDPVLGLRIG ADERIPGGIT PDDGAGLARR
     LAATGAIDHL NTSIGVATST LHLIEPSMHV PSGYAGHLAA RLRSAVRETG SDVPVIGVGR
     FTTPAQAAAA LDRGECDLVG VARGQIADPE FAAKALDGRP VRRCVGCNQD CIGRVGLNLP
     LGCTVAPAAG REWLAGPAAP DRPTRPAGAR PLRVLVAGAG PAGLSAAAAL AGRGHDVTLV
     ERAARTGGRL ALAAAAPGRA ELAHVTEDLL RAVHEAGAHV RFGTVVDRAF VDEHRPDALV
     LATGARPVPP HWDPDRLSIP VDDVLAGAPI PDGPVLVVDE LGFHQATSVA ELLAARGHET
     EIVTPALVVG QDLGLTLDRE GFRRRAHAAG IRCSTDRAVL GVLRTGEQSR AVELLHHPTG
     RIERREVSAV IAATAATAAT AATAATAPST SSLSPGPCAQ LWIPAGEDGP TVHRIGDALT
     PRRADAAIRE GAAVLT
//
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