ID A0A0A5GG04_9BACI Unreviewed; 560 AA.
AC A0A0A5GG04;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN ORFNames=N783_02420 {ECO:0000313|EMBL:KGX90020.1};
OS Pontibacillus marinus BH030004 = DSM 16465.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385511 {ECO:0000313|EMBL:KGX90020.1, ECO:0000313|Proteomes:UP000030403};
RN [1] {ECO:0000313|EMBL:KGX90020.1, ECO:0000313|Proteomes:UP000030403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030004 {ECO:0000313|EMBL:KGX90020.1,
RC ECO:0000313|Proteomes:UP000030403};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) 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:KGX90020.1}.
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DR EMBL; AVPF01000010; KGX90020.1; -; Genomic_DNA.
DR RefSeq; WP_027446331.1; NZ_AVPF01000010.1.
DR AlphaFoldDB; A0A0A5GG04; -.
DR STRING; 1385511.GCA_000425225_02653; -.
DR eggNOG; COG2303; Bacteria.
DR OrthoDB; 9785276at2; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000030403; 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; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 ECO:0000313|EMBL:KGX90020.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030403}.
FT DOMAIN 84..107
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 257..271
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 560 AA; 62207 MW; 6FEAE5597E7E08B5 CRC64;
MSEFYDIVIV GGGSAGSVLA NRLSEDGKKS VLVLEAGRSD YSWDLLIQMP AALPFPAGKS
LYDWKYESDP EPYMNGRRIK HARGKVLGGS SSINGMIYQR GNPMDYERWG ADKGMESWDF
AHCLPYFKRL ENALASPDDE LRGHDGPVKL ERGPAKNPLF QSFFDSAVQA GYSRTPDVNG
FRQEGFGPFD KHVYKGQRMS ASRAYIHPVM DRENLTVRTR AFVKHIDFDG TKAKGFTYYR
NGKTHQVEAG EVILAGGAIN TPQLLQLSGV GEAEHLLSLG IKPVVNLPGV GENLQDHLEV
YIQHACPEPV SEQPNLSKAR MPWIGLEWML KRTGPASTNH FEGGGFVRSN EDVDYPNLMF
HFLPVAVRYD GQKAPTDHGF QVHIGPMYSD ARGSLKIRST DPKEHPSMVY NYLSTEQDRR
EWIEAVRITR EIMSQPAMKK YNAGEISPGP TVQTDEEILE WVKEDAETAL HPSCTAKMGP
DSDPMAVVDP ETMKVHGTEN LRVVDASAMP YVTNGNIHAP VLMLAEKAAD LIRGEKPLDP
IHADFYRHGV HAPDAGTVTK
//
