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
//