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Database: UniProt
Entry: A0A099KY26_9GAMM
LinkDB: A0A099KY26_9GAMM
Original site: A0A099KY26_9GAMM 
ID   A0A099KY26_9GAMM        Unreviewed;       561 AA.
AC   A0A099KY26;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   08-MAY-2019, entry version 29.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   ORFNames=ND16A_1406 {ECO:0000313|EMBL:KGJ94782.1};
OS   Thalassotalea sp. ND16A.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassotalea.
OX   NCBI_TaxID=1535422 {ECO:0000313|EMBL:KGJ94782.1, ECO:0000313|Proteomes:UP000029848};
RN   [1] {ECO:0000313|EMBL:KGJ94782.1, ECO:0000313|Proteomes:UP000029848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND16A {ECO:0000313|EMBL:KGJ94782.1,
RC   ECO:0000313|Proteomes:UP000029848};
RA   Stelling S.C., Techtmann S.M., Utturkar S.M., Alshibli N., Brown S.D.,
RA   Hazen T.C.;
RT   "Draft Genome Sequence of Thalassotalea sp. strain ND16A Isolated from
RT   Eastern Mediterranean Deep Water.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant
CC       glycine betaine. Catalyzes the oxidation of choline to betaine
CC       aldehyde and betaine aldehyde to glycine betaine at the same rate.
CC       {ECO:0000256|SAAS:SAAS00321133}.
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         ECO:0000256|SAAS:SAAS01117340};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=betaine aldehyde + H2O + NAD(+) = betaine + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15710, ChEBI:CHEBI:17750,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.8;
CC         Evidence={ECO:0000256|SAAS:SAAS01117337};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2,
CC         ECO:0000256|SAAS:SAAS01080756};
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       ECO:0000256|SAAS:SAAS00321105}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|RuleBase:RU003968, ECO:0000256|SAAS:SAAS01080758}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KGJ94782.1}.
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DR   EMBL; JQDZ01000071; KGJ94782.1; -; Genomic_DNA.
DR   RefSeq; WP_033077988.1; NZ_JQDZ01000071.1.
DR   STRING; 1535422.ND16A_1406; -.
DR   EnsemblBacteria; KGJ94782; KGJ94782; ND16A_1406.
DR   PATRIC; fig|1535422.3.peg.2404; -.
DR   OrthoDB; 543793at2; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000029848; Unassembled WGS sequence.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
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:UP000029848};
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968,
KW   ECO:0000256|SAAS:SAAS01080750};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968,
KW   ECO:0000256|SAAS:SAAS01080744}; NAD {ECO:0000256|SAAS:SAAS00321145};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS01080751,
KW   ECO:0000313|EMBL:KGJ94782.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029848}.
FT   DOMAIN       83    106       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00623}.
FT   DOMAIN      256    270       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00624}.
FT   NP_BIND      93     96       FAD. {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   BINDING      85     85       FAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   BINDING     221    221       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000137-
FT                                2}.
SQ   SEQUENCE   561 AA;  62362 MW;  DFFDB54C21B6A1FE CRC64;
     MKTHLYDYII VGAGSAGCVL ANRLSEDGNS NVLLLETGGS DKSIFIQMPT ALSIPMNTSK
     YNWQFETEPE PFIDNRRMHC PRGKVLGGSS SINGMVYVRG HARDFDEWQQ HGADNWDYAH
     CLPYFKKAET WAYGADEYRG DKGPLGVNNG NEMANPLYKA FVNAGVDAGY FPTDDYNGRQ
     QEGFGAMHMT VKNGVRCSTS NAYLRPAMNR KNLTVITHAL VHKVLLENKT AVGIRYERKG
     KIVDVNVNKE VILSAGSIGS PHLLQLSGIG AKKVLTTAGI ETLHDLPGVG QNLQDHLEFY
     FQFKCKQPIS LNGKLGLWDK FLIGTRWLLF KDGLGATNHF ESCGFIRSKD SVEWPDLQYH
     FLPAAMRYDG KEAFAGHGFQ VHIGHNKPKS RGSVNVVSND PKAHPKISFN YLEHEEDRAG
     FRACVRLTRE IIHQPALDQY RGEEIQPGAH IQTDEEIDAF VRSTVESAYH PSCTCKMGND
     DLAVVDSQTR VRGIKGLRVV DSSIFPTIPN GNLNAPTIMV AERAADLIRG IETLAPSNAA
     VDIAENWQEQ QRPKEAKRKI T
//
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