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Database: UniProt
Entry: F5XFP0_MICPN
LinkDB: F5XFP0_MICPN
Original site: F5XFP0_MICPN 
ID   F5XFP0_MICPN            Unreviewed;       676 AA.
AC   F5XFP0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:BAK35447.1};
GN   OrderedLocusNames=MLP_24330 {ECO:0000313|EMBL:BAK35447.1};
OS   Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS   101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Microlunatus.
OX   NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK35447.1, ECO:0000313|Proteomes:UP000007947};
RN   [1] {ECO:0000313|EMBL:BAK35447.1, ECO:0000313|Proteomes:UP000007947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC   / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA   Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA   Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; AP012204; BAK35447.1; -; Genomic_DNA.
DR   RefSeq; WP_013863317.1; NC_015635.1.
DR   AlphaFoldDB; F5XFP0; -.
DR   STRING; 1032480.MLP_24330; -.
DR   KEGG; mph:MLP_24330; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG1902; Bacteria.
DR   HOGENOM; CLU_012153_1_2_11; -.
DR   OrthoDB; 3169239at2; -.
DR   Proteomes; UP000007947; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
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; PF00724; Oxidored_FMN; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007947}.
FT   DOMAIN          6..339
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          379..485
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   676 AA;  73824 MW;  6E3CCA38BB1BD4EE CRC64;
     MTDDPLLQPF TLGNLTLRNR IVFTPHEPAY TEDGMPKDRY LAYHLERARG GVGLIGIGGS
     AVVSKDSPAV FGNMDVTRDE IVGWLRNFGD AMHSEDAKVV IQLTHLGWRA SNILGDWLPI
     IAPSRLREPA HRSFTKAMEE FDIDRVVADY AAAAQRVKAS GLDAIELIHG GHLLDAFLLD
     RMNFRDDDYN GDLDNRLRFS LKVIDGIRAA VGDDFVVGVK MVFTDDADGG MREDLATEIA
     KRYVDHGIDF INLVVGSTSS DAELSRNIPG MGTPSAPNLE ICRRVRAQLS VPLLHATRIT
     DAATARFAIE DGCVDLVGMT RAHIADPYLV RKIAEKRDDD IRPCVGANAC LDAIYVSGSA
     TCIHNPATGR EQTLPQLEPA SPQPGKRVVV VGAGPAGLEA ARVCAVRGHQ VTVLEADSTY
     GGQVRIAARS KHRRDLIGIV DWRYQQAVKH GVDFRFDVLA EPEDILAENP DVVIIATGGI
     PDTDYGDVRA EVNDVWDVMQ DSLKSKKRVI VFDDHGFYPA LDAVERLATN GQEVIYVTPE
     RAIGVDVGGM NSPEYLKTFS TYGVQTVLNE RLIKTTRGEG RTVVATLRNE YSDRETELRA
     DALVIDHGTN PNDELYFALK DASRNGGDLD RTALVAGELQ PPVDGDGFLL YRIGDAVSSR
     NVHAALLDAL RIGMGL
//
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