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Database: UniProt
Entry: A0A1J4NXV1_9ACTN
LinkDB: A0A1J4NXV1_9ACTN
Original site: A0A1J4NXV1_9ACTN 
ID   A0A1J4NXV1_9ACTN        Unreviewed;       556 AA.
AC   A0A1J4NXV1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   08-MAY-2019, entry version 13.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   ORFNames=WN71_013395 {ECO:0000313|EMBL:OIJ67361.1};
OS   Streptomyces mangrovisoli.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1428628 {ECO:0000313|EMBL:OIJ67361.1, ECO:0000313|Proteomes:UP000034196};
RN   [1] {ECO:0000313|EMBL:OIJ67361.1, ECO:0000313|Proteomes:UP000034196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC149T {ECO:0000313|Proteomes:UP000034196};
RA   Lee L.-H., Ser H.-L.;
RT   "Genome sequence of Streptomyces mangrovisoli MUSC 149.";
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}.
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:OIJ67361.1}.
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DR   EMBL; LAVA02000027; OIJ67361.1; -; Genomic_DNA.
DR   RefSeq; WP_046586174.1; NZ_LAVA02000027.1.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000034196; 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:UP000034196};
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:UP000034196}.
FT   DOMAIN       85    108       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00623}.
FT   DOMAIN      260    274       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00624}.
FT   BINDING      87     87       FAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   BINDING     225    225       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000137-
FT                                2}.
SQ   SEQUENCE   556 AA;  61078 MW;  023D9A34D48D8186 CRC64;
     MASLHHDFVI VGGGSAGCAL AARLSADPGN RVLVLEAGRS DYPWDVFIHM PAALTHPIGN
     RFYDWKYESE PEPHMNGRRI YHARGKVLGG SSSINGMIFQ RGNPLDYERW AADPGMESWD
     YAHCLPYFRR MENCLAADPD DEFRGHDGPL VLERGPATNP LFGAFLEAVE QAGQFRTDDV
     NGYRQEGFAP FDRTLHRGRR LSAARAYLDP VRGRPNLTVV TRAFVERILF EGDRAVGVEY
     RRGRGAPRQV RAAEVVLCGG AVNSPQLLQL SGVGNATELA ALGVDVVHDL PGVGENLQDH
     LEVYVQYACT RPVSMQPYMA KWRAPFIGLQ WLFRKGPGAT NHFEAGGFAR SNDDVGYPNL
     MFHFLPLAVR YDGSAPAGGH GYQVHVGPMY SDARGSVKIR SSDPREHPAL RFNYLSTEQD
     RREWVEAIRV ARTLLAQPAL APYNGGEISP GPAVESDEEI LAWVAREGET ALHPSCTCKM
     GTDAMAVVDP LTLRVHGLDG LRVVDASVMP YVTNGNIYAP VMMIAEKAAD LILGNEPPAP
     SGAVYYRRNQ ARTQAS
//
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