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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//