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Database: UniProt
Entry: A0A2I4ANZ9_9TELE
LinkDB: A0A2I4ANZ9_9TELE
Original site: A0A2I4ANZ9_9TELE 
ID   A0A2I4ANZ9_9TELE        Unreviewed;       606 AA.
AC   A0A2I4ANZ9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   16-JAN-2019, entry version 7.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   Name=chdh {ECO:0000313|RefSeq:XP_013857186.1};
OS   Austrofundulus limnaeus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae;
OC   Austrofundulus.
OX   NCBI_TaxID=52670 {ECO:0000313|Proteomes:UP000192220, ECO:0000313|RefSeq:XP_013857186.1};
RN   [1] {ECO:0000313|RefSeq:XP_013857186.1}
RP   IDENTIFICATION.
RC   STRAIN=Quisiro {ECO:0000313|RefSeq:XP_013857186.1};
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_013857186.1};
RG   RefSeq;
RL   Submitted (JAN-2018) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + choline = AH2 + betaine aldehyde;
CC         Xref=Rhea:RHEA:17433, ChEBI:CHEBI:13193, ChEBI:CHEBI:15354,
CC         ChEBI:CHEBI:15710, 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|PIRSR:PIRSR000137-2};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis
CC       via choline pathway; betaine aldehyde from choline (cytochrome c
CC       reductase route): step 1/1. {ECO:0000256|RuleBase:RU003969}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|RuleBase:RU003968}.
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DR   RefSeq; XP_013857186.1; XM_014001732.1.
DR   GeneID; 106513072; -.
DR   CTD; 55349; -.
DR   OrthoDB; 798314at2759; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000192220; Genome assembly.
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; -; 1.
DR   Gene3D; 4.10.450.10; -; 1.
DR   InterPro; IPR011533; BetA.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027424; Glucose_Oxidase_domain_2.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01810; betA; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000192220};
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192220}.
FT   DOMAIN      137    160       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00623}.
FT   DOMAIN      309    323       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00624}.
FT   NP_BIND     147    150       FAD. {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   BINDING     139    139       FAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000137-2}.
SQ   SEQUENCE   606 AA;  67658 MW;  FDDFBB9E87F276FB CRC64;
     MMLSLATVGQ AGARRVLTQT WVKFIKDGRC FTASAFHRYS STSPSANQKT PSYSYVIIGA
     GSAGCVLANR LSEDAHESVL LLEAGPKDKL LGSSRLSWKI HMPAALTYNL CDDKYNWFYH
     TLPQANMDNR VLYWPRGRVW GGSSSLNAMV YIRGHAEDYN RWQREGAEGW DYKHCLPYFR
     KAQCHELGQN MYRGGDGPLH VSRGKTNHPL HKAFIEAGQQ AGYPFTDDMN GYQQEGVGWM
     DMTVYKGKRW STASAYLRPA LGRPNLKAEV RCLTTKILFD GRRAVGVEYM QNGQKKRVFA
     DKEVILSGGA INSPQLLMLS GVGNADDLKD LGIPVVQHLP GVGSNLQDHL ELYVQQQCTQ
     PITLYKAQKP FHMIKIGLEW LSLFTGYGAT SHLESGGFIR SRPKVAHPDI QFHFLPSQVI
     DHGRVPSEIE AYQVHVGPMR STSIGWMKLK STSPLDHPIL QPNYLSTEID VWEFRQCVKL
     SREIFAQKAF DPFRGPEFQP GPQVQSDAEI DAFVRQKADS AYHPSCTCKM GSPSDPMTVV
     NSNTQVLGLE RLRVVDASIM PSVVSGNLNA PTIMIAEKTA DKIRGRPALV DPEVPVYKPP
     TLETQR
//
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