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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   24-JAN-2024, entry version 26.
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; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + choline = AH2 + betaine aldehyde; Xref=Rhea:RHEA:17433,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15354, ChEBI:CHEBI:15710,
CC         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|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       choline pathway; betaine aldehyde from choline (cytochrome c reductase
CC       route): step 1/1. {ECO:0000256|RuleBase:RU003969}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {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   AlphaFoldDB; A0A1J4NXV1; -.
DR   STRING; 1428628.WN71_013395; -.
DR   OrthoDB; 9785276at2; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000034196; Unassembled WGS sequence.
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; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR011533; BetA.
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   NCBIfam; TIGR01810; betA; 1.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034196}.
FT   DOMAIN          85..108
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          260..274
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         87
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         225
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
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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