ID A0A1M5RE73_9ACTN Unreviewed; 546 AA.
AC A0A1M5RE73;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SHH24564.1};
GN ORFNames=SAMN05443575_3523 {ECO:0000313|EMBL:SHH24564.1};
OS Jatrophihabitans endophyticus.
OC Bacteria; Actinomycetota; Actinomycetes; Jatrophihabitantales;
OC Jatrophihabitantaceae; Jatrophihabitans.
OX NCBI_TaxID=1206085 {ECO:0000313|EMBL:SHH24564.1, ECO:0000313|Proteomes:UP000186132};
RN [1] {ECO:0000313|EMBL:SHH24564.1, ECO:0000313|Proteomes:UP000186132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45627 {ECO:0000313|EMBL:SHH24564.1,
RC ECO:0000313|Proteomes:UP000186132};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; FQVU01000005; SHH24564.1; -; Genomic_DNA.
DR RefSeq; WP_073391943.1; NZ_FQVU01000005.1.
DR AlphaFoldDB; A0A1M5RE73; -.
DR STRING; 1206085.SAMN05443575_3523; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000186132; Unassembled WGS sequence.
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; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000186132}.
FT DOMAIN 85..108
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT ACT_SITE 471
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 513
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 546 AA; 56416 MW; 1227DFB8C7330E7C CRC64;
MTGAGTLVAD YVVVGAGSAG CVLASRLSAV PDTSVVLVEA GDADRRAELS VPAAYPRLFG
TSADWGFETV AQPGLGGRRV AWPRGRVLGG SSALNAQIWT RGHPADFDAW AAAGCSGWAW
ADVLPYFCRA EQLTGAVATA PAERPSPRVD RPGALGRHGS VRLTGLRDPS PATAAFLAAC
AQAGLPRLAA EGDGRDEGYA PVLVTQHHGR RWSAVDAYLR PAAGRDSLTV LTGARLRAIT
FDAAAATGVE VVTAAGVVHV AARREVLLAA GAIGSPWALL DAGIGDAAAL RAAGRPVRVH
RPEVGRNLAD HLYVPVSATS PHALSPGVGD QRAGAAEYLA RRRGPLTSNL AEALAFVRTD
PALVAPDIEL LWLVVPRLDQ PSRHGVTVAS VLLQPASRGR VALDPAAPDA APVIDAGYLT
DPDGADLTTL LRGVARARQV LTRPALAAWC DPDLAGGDVA LCRGSAQTLY HPVGTCRMGA
DADAVLDPQL RVRGVERLRV VDASAMPTIT RAHTQAPTVM LAERAADLVV ADSPARRERA
PAGVPG
//
