ID A0A1C5A4T0_MICEC Unreviewed; 505 AA.
AC A0A1C5A4T0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SCF40232.1};
GN ORFNames=GA0070618_6310 {ECO:0000313|EMBL:SCF40232.1};
OS Micromonospora echinospora (Micromonospora purpurea).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1877 {ECO:0000313|EMBL:SCF40232.1, ECO:0000313|Proteomes:UP000198253};
RN [1] {ECO:0000313|EMBL:SCF40232.1, ECO:0000313|Proteomes:UP000198253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43816 {ECO:0000313|EMBL:SCF40232.1,
RC ECO:0000313|Proteomes:UP000198253};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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; LT607413; SCF40232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5A4T0; -.
DR InParanoid; A0A1C5A4T0; -.
DR Proteomes; UP000198253; Chromosome i.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 235..295
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 374..495
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 505 AA; 53174 MW; B2B0CED9A238DD81 CRC64;
MTAPDSTTDL LIIGSGIMGS VVARLVREAS TATSIVMVDG GPPIGAMPGL HVHDTADPQI
WAQYNSPLAS GIQSFYTGVE PPPSQSPDAY RLKAGLHLLS AVGNDTSAMP AAAAAWNVGG
MGAHWTAVTP WPAGTEVFDH GDPGLWQRDL NTARRALGVT SAAIGPTLPG EVVLAELRRR
YRGVGPADRA PQLMPMAVTR EPGGRLLRTG PSRIFPPLGS GGDSRFTLLP RTLAVALDHD
GRRVRGAVVL DVETGDRRVI EATATVVCAD AFRTPQLLFA SGIRPPALGR YLNEHAFLTG
RVLLDLDRFG LDRAGLPRAA GDERNTDSLW LPQNGPAQPF HGQIMNTTYV DPEGLPLAHA
VGLSLFSPVE TRPENGIRFS EDTTDVTGMP SFEIEFGYTD ADLNLIGAGR SELRAIAERF
GDFDPGTESA LLPPGSSLHL TGTVRMGTAD DGTSVCDPYG QVWAFDNLYL AGNGVVPTAV
VGNSTLTGTV TAVRAARAAL RTIAA
//