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Database: UniProt
Entry: W2PSU1_PHYPN
LinkDB: W2PSU1_PHYPN
Original site: W2PSU1_PHYPN 
ID   W2PSU1_PHYPN            Unreviewed;       587 AA.
AC   W2PSU1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   ORFNames=PPTG_15925 {ECO:0000313|EMBL:ETN03711.1};
OS   Phytophthora parasitica (strain INRA-310).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN03711.1, ECO:0000313|Proteomes:UP000018817};
RN   [1] {ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETN03711.1, ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|EMBL:ETN03711.1,
RC   ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + choline = AH2 + betaine aldehyde; Xref=Rhea:RHEA:17433,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15354, ChEBI:CHEBI:15710,
CC         ChEBI:CHEBI:17499; EC=1.1.99.1;
CC         Evidence={ECO:0000256|RuleBase:RU003969};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       choline pathway; betaine aldehyde from choline (cytochrome c reductase
CC       route): step 1/1. {ECO:0000256|RuleBase:RU003969}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; KI669609; ETN03711.1; -; Genomic_DNA.
DR   RefSeq; XP_008910938.1; XM_008912690.1.
DR   AlphaFoldDB; W2PSU1; -.
DR   STRING; 761204.W2PSU1; -.
DR   EnsemblProtists; ETN03711; ETN03711; PPTG_15925.
DR   GeneID; 20185039; -.
DR   VEuPathDB; FungiDB:PPTG_15925; -.
DR   OMA; NHFESCA; -.
DR   OrthoDB; 3382025at2759; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000018817; Unassembled WGS sequence.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
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; IPR011533; BetA.
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   NCBIfam; TIGR01810; betA; 1.
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.
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,
KW   ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018817}.
FT   DOMAIN          115..138
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          290..304
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          568..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         117
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         125..128
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         253
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   587 AA;  65722 MW;  C56FCB53DB56B036 CRC64;
     MLRHSLRSSA SALQQRASPV AARALSSSAA NAEYDYVIVG GGSAGCVLAN RLTEDPNNKV
     LLVETGPDDR TKWDSWKIHM PAALTYNLAN DKYNWYYFTE PQKHLNNRRL PWPRGRVLGG
     SSSLNAMVYI RGHAYDYDDW QESGADGWSY ADCLPYFRKA QNHELGPDDY RGGDGPLHVI
     RGNQKDQVLF KKFIDAGVQA GYPFTEDMNG YQQEGFGWMD MTVWKGFRWS TASAYLRPAM
     KRPNLTVVTD TFVSKVVFEG KKAVGVETEN RKNKTTKQVR AAKEVILSGG AINSPQLLML
     SGIGDADHLK EVGVPVVQHL PAVGQNMEDH LDLYVQYMCK KPITLHNATW KYPHKMVAIG
     LEWIFRQTGM GASSHLESGG FIRSAPGKRH PDLQYHFLPG SLTGQLTPGA YHAMQAHCSP
     MRAQSRGWLK LRSNNPHEHP IIEPNYLSEE QDLVDMRNGV KLTREILEQQ TLDEYRGDPI
     SPSKDVQTDA QIDEWIRQHT ESAYHPSCTN RMGVDENTVV DPQTRVHGVE NLRVVDASIM
     PNIVSGNLNA PTIMIAEKAA DIILGKTPLP KSTAPVYQPK NWETSQR
//
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