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Database: UniProt
Entry: A0A1W6CWE3_9RHOB
LinkDB: A0A1W6CWE3_9RHOB
Original site: A0A1W6CWE3_9RHOB 
ID   A0A1W6CWE3_9RHOB        Unreviewed;       678 AA.
AC   A0A1W6CWE3;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=N-methylproline demethylase {ECO:0000313|EMBL:ARJ69171.1};
GN   ORFNames=B0A89_05590 {ECO:0000313|EMBL:ARJ69171.1};
OS   Paracoccus contaminans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1945662 {ECO:0000313|EMBL:ARJ69171.1, ECO:0000313|Proteomes:UP000193017};
RN   [1] {ECO:0000313|EMBL:ARJ69171.1, ECO:0000313|Proteomes:UP000193017}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKI 16-01929T\LMG 29738T\CCM 8701T\CIP 111112T
RC   {ECO:0000313|Proteomes:UP000193017};
RA   Aurass P., Karste S., Trost E., Glaeser S.P., Kaempfer P., Flieger A.;
RT   "Genome sequence of Paracoccus contaminans isolated from a water
RT   microcosm.";
RL   Submitted (MAR-2017) 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; CP020612; ARJ69171.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6CWE3; -.
DR   STRING; 1945662.B0A89_05590; -.
DR   KEGG; pcon:B0A89_05590; -.
DR   OrthoDB; 9784632at2; -.
DR   Proteomes; UP000193017; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd04734; OYE_like_3_FMN; 1.
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; 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; PF13450; NAD_binding_8; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000313|EMBL:ARJ69171.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193017};
KW   Transferase {ECO:0000313|EMBL:ARJ69171.1}.
FT   DOMAIN          6..339
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
SQ   SEQUENCE   678 AA;  73939 MW;  DF9A381E6359C596 CRC64;
     MSTDPLLQPF QLRHLTLKNR LLLTSHEPAY GEDGLPKDRY RAYHVERAKG GVALTMTAGS
     AVVGPDSPPA FGNLLLYKDE VVPWMKRLVD ECHDHGAAVM IQVTHMGRRT RWDRGDWLPV
     LGPSHEREAA HRAFPKRIED WDIARIVTQF ADAAERMKAA GVDGIELQAY GQLLAQFWTP
     SINDLGPPYG GNLENRLRFT FEVLDAIRAR VGPDFIVGMR VVPDEQMPGG VTREDGAEIA
     RLLRGTGQVD FLNIVRGHID TDAGLTDLIP IHGMPSAPHL DFAGEIRAST RMPTFHAARI
     QDVATARHAV ASGLLDMVGM TRAHIADPHI VRKIMAGAED RIRPCVGANY CLDRIYQGGM
     ALCIHNAASG REETLPHAAA PAARPRRVTI VGAGPAGLEA ARVAAERGHA VTVFEAADQP
     GGQVRLAALQ PRRRELGQII SWRQAECDRM GVAFHFNSYA EAGEVLDTDP EVVIVATGGL
     PHTEVLAQGN ELVVSAWDIL SGDMRPGANV LVFDDAGDHA ALQAAQAIAE TGAAVEIVTP
     DRSFAPEIMA MNLVPYMRAL QKGQTTFTVT WRLRAVVREG NLLRVTLGSD YGEAARERLV
     DQVVVNHGTR PLDELYFDLK PLSSNLGEVD YGAMIAGHPQ QVVRNPEGRF QLFRIGDAVS
     ARNTHAAVHD ALRLVKDL
//
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