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Database: UniProt
Entry: A0A0Q9PZJ9_9ACTN
LinkDB: A0A0Q9PZJ9_9ACTN
Original site: A0A0Q9PZJ9_9ACTN 
ID   A0A0Q9PZJ9_9ACTN        Unreviewed;       527 AA.
AC   A0A0Q9PZJ9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:KRE96109.1};
GN   ORFNames=ASG76_03430 {ECO:0000313|EMBL:KRE96109.1};
OS   Nocardioides sp. Soil774.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736408 {ECO:0000313|EMBL:KRE96109.1, ECO:0000313|Proteomes:UP000051100};
RN   [1] {ECO:0000313|EMBL:KRE96109.1, ECO:0000313|Proteomes:UP000051100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil774 {ECO:0000313|EMBL:KRE96109.1,
RC   ECO:0000313|Proteomes:UP000051100};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE96109.1, ECO:0000313|Proteomes:UP000051100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil774 {ECO:0000313|EMBL:KRE96109.1,
RC   ECO:0000313|Proteomes:UP000051100};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRE96109.1}.
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DR   EMBL; LMSM01000005; KRE96109.1; -; Genomic_DNA.
DR   RefSeq; WP_056600444.1; NZ_LMSM01000005.1.
DR   AlphaFoldDB; A0A0Q9PZJ9; -.
DR   STRING; 1736408.ASG76_03430; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000051100; 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; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          255..269
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         220
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   527 AA;  57161 MW;  F8FF056ECE4DC7E7 CRC64;
     MPEETFDYIV IGSGSAGGVV AARLSEDPQV RVLLLEAGPA DDDDNIHMPL AFSMLFKTKW
     DWNYETTPQK HLDGRRAYWP RMKALGGCSS MNAMIYIRGN HADYDEWRDA YGATGWGFDD
     VLPYFVRAEG NTRLGGPFHG TDGPLHVEDR SYNHELSTAF IEAGVAAGLK RNDDFNGAEQ
     EGVGLYQVTC KKGRRWSVAD AYIHPASSRP NLVVRTEAFV TRIVLEGTRA VGVAYTRGGQ
     DHVVRAEAEV VLSGGAINSP QLLMLSGIGP GAHLRDMGID VVVESPGVGQ HLQDHPVSGI
     LSYTKDTTDV AEMLGLGNLV KWKALGKGPL SSNVAETGAF YRSHESLDLP DIQLHVAPTG
     FYDNGMHEPV RRALTTAVTL VNVQSSGHVR LRSADPTWHP EIDPGYFDDR ADLEAMIGGF
     RTALEVLRQG PIATYVAEPW VPASADPSDD EIIEAIGRLG QTLYHPVATC AMGTVEGSVV
     DPELRVHGVE GLRVADASVM PRVPRGNTNA PTIMIGEKCA DLLKESR
//
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