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Database: UniProt
Entry: A0A1G8LLQ7_9RHOB
LinkDB: A0A1G8LLQ7_9RHOB
Original site: A0A1G8LLQ7_9RHOB 
ID   A0A1G8LLQ7_9RHOB        Unreviewed;       552 AA.
AC   A0A1G8LLQ7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   08-MAY-2019, entry version 10.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   ORFNames=SAMN04488026_100484 {ECO:0000313|EMBL:SDI56606.1};
OS   Pseudoruegeria lutimaris.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Pseudoruegeria.
OX   NCBI_TaxID=571298 {ECO:0000313|EMBL:SDI56606.1, ECO:0000313|Proteomes:UP000199382};
RN   [1] {ECO:0000313|EMBL:SDI56606.1, ECO:0000313|Proteomes:UP000199382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25294 {ECO:0000313|EMBL:SDI56606.1,
RC   ECO:0000313|Proteomes:UP000199382};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNEK01000004; SDI56606.1; -; Genomic_DNA.
DR   BioCyc; GCF_900099935:BLR85_RS03400-MONOMER; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000199382; 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:UP000199382};
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   Reference proteome {ECO:0000313|Proteomes:UP000199382}.
FT   DOMAIN       79    102       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00623}.
FT   DOMAIN      254    268       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00624}.
FT   NP_BIND      89     92       FAD. {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   BINDING      81     81       FAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000137-2}.
SQ   SEQUENCE   552 AA;  60890 MW;  62EC67AA55992923 CRC64;
     MQAEYVVIGA GSAGCATAYR LAEAGRKVLV IEHGVSDWGP FIQMPAALSY PMNMPLYDWG
     FQTEPEPHLG GRRLATPRGK VVGGSSSVNG MVYVRGHAGD FDHWAEAGAE GWSFADVLPY
     FKRMEHWHDG GHGGDPDWRG TDGPLHVTRG PRTNPLHAAF VEAGQQAGYE VTEDYNGEKQ
     EGFGVMEQNV WKGRRWSTAN AYLKPALKQE NCTLVRAFAR RIVVEDGRAV GVEVERGGKV
     EVIRAEREVI LAASSINSPK LLMLSGIGPA AHLAEHGIDV VADRPGVGQN LQDHLEVYIQ
     MAAREPITLY KYWNLWGKAL IGAQWLFTRT GLGASNQFES AAFIRSQAGV DYPDIQYHFL
     PIAVRYDGKA AAEGHGFQAH TGPMRSPSRG EITLRSADPK EAPRIFFNYM STEQDWVDFR
     RCIRLTREIF AQDAFKPFVK HEIQPGDALT SDDEIDGFIR EHAESAYHPC GSCRMGRKDD
     PGAVVDSECR VIGVDGLRLA DSSIFPRITN GNLNAPAIMV GEKAADHILG RTPLAPENIA
     PWRHPDWQVA QR
//
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