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
//