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Database: UniProt
Entry: C5L0Z1_PERM5
LinkDB: C5L0Z1_PERM5
Original site: C5L0Z1_PERM5 
ID   C5L0Z1_PERM5            Unreviewed;       599 AA.
AC   C5L0Z1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Choline dehydrogenase, putative {ECO:0000313|EMBL:EER09633.1};
GN   ORFNames=Pmar_PMAR008773 {ECO:0000313|EMBL:EER09633.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EER09633.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) 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}.
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DR   EMBL; GG678140; EER09633.1; -; Genomic_DNA.
DR   RefSeq; XP_002777838.1; XM_002777792.1.
DR   AlphaFoldDB; C5L0Z1; -.
DR   EnsemblProtists; EER09633; EER09633; Pmar_PMAR008773.
DR   GeneID; 9052557; -.
DR   InParanoid; C5L0Z1; -.
DR   OMA; NHFESCA; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000007800; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800}.
FT   DOMAIN          297..311
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         109..112
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         255
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   599 AA;  66923 MW;  2E7776C7B11F9405 CRC64;
     MLSQSPLRCL SVAAASHFDY IILGAGSAGC VMANRLSEDP NVKVAVLEAG RWHRGSWDWW
     KAAMPAALTF NLANKKYNWD YHTVPQKHMN NRRLHQPRGK MTGGSSGINA MVYVRGHALD
     FERWASQEGC PGWSYRDVLP YFKKSTTHEL GENFYRGGAG PIHVRRGATG NELFKAFVDA
     GVQAGYPYTE DMNGKQQEGF GPMDMTVSPV DSSETPFELS RFKVTSDGKR CHAGLAYLNE
     AAKRPNCSVI TRAMVNRLVW ERSPDGAEKR CIGVEYIDHV GEPRYIKAGR EIIMAMGAVG
     TPQILNLSGV GDPDHLRSLS IDPVIANQNV GQNLQDHLEF YVQYLCSKPV SLFPVATWRY
     PHLKALTGIE WLLKGTGLAA SNHFDTGGFI RTRAGIRHPD FQFHFIPGCV VGQLDFLPHH
     GYQAHGGTMR PKSRGAIKIT SKDPRDEPLI DPNFLADVED MRDMREGLRR TIEIMEQPAL
     KDYYMESRLS PATDFNLDSD DDCDRWIKNS SHSAYHLSCT AAMGKVVDEH GRLYGASNVR
     VVDASAMPSM TSGNLNAPTL MMAEKFADHI RGRPYLDPAQ SENDEALWWE NPTWQTSQR
//
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