ID A0A364V744_9CORY Unreviewed; 595 AA.
AC A0A364V744;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN Name=betA {ECO:0000313|EMBL:RAV32376.1};
GN ORFNames=DLJ54_03600 {ECO:0000313|EMBL:RAV32376.1};
OS Corynebacterium heidelbergense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=2055947 {ECO:0000313|EMBL:RAV32376.1, ECO:0000313|Proteomes:UP000251577};
RN [1] {ECO:0000313|EMBL:RAV32376.1, ECO:0000313|Proteomes:UP000251577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=647 {ECO:0000313|EMBL:RAV32376.1,
RC ECO:0000313|Proteomes:UP000251577};
RX PubMed=29958724;
RA Braun M.S., Wang E., Zimmermann S., Wink M.;
RT "Corynebacterium heidelbergense sp. nov., isolated from the preen glands of
RT Egyptian geese (Alopochen aegyptiacus).";
RL Syst. Appl. Microbiol. 0:0-0(2018).
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:RAV32376.1}.
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DR EMBL; QHCV01000025; RAV32376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364V744; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000251577; 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:UP000251577}.
FT DOMAIN 105..128
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 279..293
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 595 AA; 66266 MW; F5685D7FEFD63B81 CRC64;
MALTKKIRAA YSRHDRSGEV IEDRRRDVVI VGGGSAGCVL ANRLSENART EVLVLEAGRP
DSLWDLFIHM PAAFSFPIGD KHYDWMYESA PEPEMNGRRI YHARGKVLGG SSSVNGMIFQ
RGNPMDYEKW GALKGMGNWD FAHVLPYFNR METALGAEPG DPRRGHSGPL KLTRGPATSP
LFQAFFRSVQ QAGYNLTNDV NGYRQEGFAP FDRNILGGKR LSAARAYLHP VMGRKNLDVR
TRALTTKVLF EGTRAVGVEY EWKGAKRRVY ADKVILCGGA FNTPQLLQVS GVGPKEVLEK
AGVPVRKDLP GVGENLQDHL EVYVQYNVTK PVSSQPYLKK WRRPFLGLQW LLTKKGPVAT
SHFEAGGFAR SNDAEDYPNL MFHFLPMAVR YDGTQPEGTH GFQFHVGPMY SDTLGHVHIT
SPDPKVKPEI IFNYLATDQD RREWVEAVRV SRRLLDTPAM KEYTDGEISP GPQVETDEEI
LEWVRNDAET ALHPSCTAKM GPAEDPMAVV DPDSMQVHGC ENLYVVDASV MPIITNGNIY
APVMMLAEKA ADLIRGRKPL NPVNVPFYRA KQDMPLYAEG EAVRDHTQAI PGAAD
//
