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Database: UniProt
Entry: A0A2K5DQT5_AOTNA
LinkDB: A0A2K5DQT5_AOTNA
Original site: A0A2K5DQT5_AOTNA 
ID   A0A2K5DQT5_AOTNA        Unreviewed;       594 AA.
AC   A0A2K5DQT5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|Ensembl:ENSANAP00000023336.1};
GN   Name=CHDH {ECO:0000313|Ensembl:ENSANAP00000023336.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000023336.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000023336.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   RefSeq; XP_012316175.1; XM_012460752.1.
DR   RefSeq; XP_012316176.1; XM_012460753.1.
DR   RefSeq; XP_012316177.1; XM_012460754.1.
DR   RefSeq; XP_012316178.1; XM_012460755.1.
DR   RefSeq; XP_012316179.1; XM_012460756.1.
DR   RefSeq; XP_012316180.1; XM_012460757.1.
DR   AlphaFoldDB; A0A2K5DQT5; -.
DR   STRING; 37293.ENSANAP00000023336; -.
DR   Ensembl; ENSANAT00000041244.1; ENSANAP00000023336.1; ENSANAG00000029420.1.
DR   GeneID; 105722925; -.
DR   CTD; 55349; -.
DR   GeneTree; ENSGT00530000063260; -.
DR   OMA; NHFESCA; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000233020; Unplaced.
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.
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   Reference proteome {ECO:0000313|Proteomes:UP000233020}.
FT   DOMAIN          125..148
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          297..311
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         127
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         135..138
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         262
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   594 AA;  65461 MW;  9EBE41F807F14F21 CRC64;
     MWCLLRGLGR PRALALGAMG RQHPPGARTL ASAGSEIRDE YSYVVVGAGS AGCVLAGRLT
     EDPAERVLLL EAGPKDLRAG SKRLSWKIHM PAALVANLCD DRYNWCYHTE AQPGLDGRVL
     YWPRGRVWGG SSSLNAMVYV RGHAEDYERW QRQGALGWDY AHCLPYFRKA QGHELGANLY
     RGADGPLRVS RGKTNHPLHR AFLEATQQAG YPLTEDMNGF QQEGFGWMDM TIHEGKRWST
     ACAYLHPALS RTNLKAEAQT LVSRVLFEGT RAVGVDYVKN GQSCRAYASK EVILSGGAIN
     SPQLLMLSGV GNADDLKKLG IPVVCHLPGV GQNLQDHLEI YIQQACTRPI TLHSAQKPLR
     KARIGLEWLW KFTGEGATAH LETGGFIRSQ PGVPHPDIQF HFLPSQVIDH GRVPTQQEAY
     QVHVGTMRGT SVGWLKLRSA NPQDHPVIQP NYLSTETDVE DFRLCVKLTR EIFAQKALAP
     FRGKELQPGS HVQSDKEIDA FVRAKADSAY HPSCTCKMGQ PSDPTAVVDP QTRVLGVENL
     RVVDASIMPS LVSGNLNAPT IMIAEKAADI IKGRPALWDK DVPVYKPRTL ATQR
//
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