ID G0AJ48_COLFT Unreviewed; 569 AA.
AC G0AJ48;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Oxygen-dependent choline dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00750};
DE Short=CDH {ECO:0000256|HAMAP-Rule:MF_00750};
DE Short=CHD {ECO:0000256|HAMAP-Rule:MF_00750};
DE EC=1.1.99.1 {ECO:0000256|HAMAP-Rule:MF_00750};
DE AltName: Full=Betaine aldehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00750};
DE Short=BADH {ECO:0000256|HAMAP-Rule:MF_00750};
DE EC=1.2.1.8 {ECO:0000256|HAMAP-Rule:MF_00750};
GN Name=betA {ECO:0000256|HAMAP-Rule:MF_00750,
GN ECO:0000313|EMBL:AEK60982.1};
GN OrderedLocusNames=CFU_1150 {ECO:0000313|EMBL:AEK60982.1};
OS Collimonas fungivorans (strain Ter331).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=1005048 {ECO:0000313|EMBL:AEK60982.1, ECO:0000313|Proteomes:UP000008392};
RN [1] {ECO:0000313|EMBL:AEK60982.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60982.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=15305924; DOI=10.1111/j.1462-2920.2004.00673.x;
RA Leveau J.H., Gerards S., de Boer W., van Veen J.A.;
RT "Phylogeny-function analysis of (meta)genomic libraries: screening for
RT expression of ribosomal RNA genes by large-insert library fluorescent in
RT situ hybridization (LIL-FISH).";
RL Environ. Microbiol. 6:990-998(2004).
RN [2] {ECO:0000313|EMBL:AEK60982.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60982.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=16457898; DOI=10.1016/j.mimet.2005.12.010;
RA Leveau J.H., Gerards S., Fritsche K., Zondag G., van Veen J.A.;
RT "Genomic flank-sequencing of plasposon insertion sites for rapid
RT identification of functional genes.";
RL J. Microbiol. Methods 66:276-285(2006).
RN [3] {ECO:0000313|EMBL:AEK60982.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60982.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=18671744; DOI=10.1111/j.1574-6941.2008.00547.x;
RA Fritsche K., de Boer W., Gerards S., van den Berg M., van Veen J.A.,
RA Leveau J.H.;
RT "Identification and characterization of genes underlying chitinolysis in
RT Collimonas fungivorans Ter331.";
RL FEMS Microbiol. Ecol. 66:123-135(2008).
RN [4] {ECO:0000313|EMBL:AEK60982.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60982.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=19638176; DOI=10.1111/j.1462-2920.2009.02010.x;
RA Leveau J.H., Uroz S., de Boer W.;
RT "The bacterial genus Collimonas: mycophagy, weathering and other adaptive
RT solutions to life in oligotrophic soil environments.";
RL Environ. Microbiol. 12:281-292(2010).
RN [5] {ECO:0000313|EMBL:AEK60982.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60982.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=21614084; DOI=10.1038/ismej.2011.29;
RA Mela F., Fritsche K., de Boer W., van Veen J.A., de Graaff L.H.,
RA van den Berg M., Leveau J.H.;
RT "Dual transcriptional profiling of a bacterial/fungal confrontation:
RT Collimonas fungivorans versus Aspergillus niger.";
RL ISME J. 5:1494-1504(2011).
RN [6] {ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|Proteomes:UP000008392};
RA Leveau J.H.;
RT "Complete sequence of Collimonas fungivorans Ter331.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC betaine. Catalyzes the oxidation of choline to betaine aldehyde and
CC betaine aldehyde to glycine betaine at the same rate.
CC {ECO:0000256|HAMAP-Rule:MF_00750}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00750, ECO:0000256|RuleBase:RU003969};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.8; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00750};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_00750};
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|HAMAP-Rule:MF_00750,
CC ECO:0000256|RuleBase:RU003969}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|HAMAP-Rule:MF_00750,
CC ECO:0000256|RuleBase:RU003968}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002745; AEK60982.1; -; Genomic_DNA.
DR AlphaFoldDB; G0AJ48; -.
DR STRING; 1005048.CFU_1150; -.
DR KEGG; cfu:CFU_1150; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_4; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000008392; Chromosome.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR HAMAP; MF_00750; Choline_dehydrogen; 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|HAMAP-Rule:MF_00750};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00750}; NAD {ECO:0000256|HAMAP-Rule:MF_00750};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00750}; Reference proteome {ECO:0000313|Proteomes:UP000008392}.
FT DOMAIN 98..121
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 273..287
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 487
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00750"
FT BINDING 20..49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00750"
SQ SEQUENCE 569 AA; 62990 MW; 6142C07129A78A52 CRC64;
MPPSRHRQGR ITMQQAKEYD YIIIGAGSAG NVLATRLTED ADTSVLLLEA GGPDYRFDFR
TQMPAALAFP LQGRRYNWAY ETDPEPHMNN RRMECGRGKG LGGSSLINGM CYIRGNALDY
DHWAKREGLE NWSYLDCLPY FKKAETRDIG GNDYHGGDGP LSVTTPKSGN NVLYHAMVEA
GVQAGYPRTD DLNGYQQEGF GPMDRTTTPR GRRASTARGY LDQARARPNL TIVTHALTDR
ILFSGKRAVG VAYLHNDQPQ TAQARREVLL CSGAIASPQI LQRSGVGPAA LLRQHDIPVV
LDLPGVGANL QDHLEIYQQY ECKQPVSLAP ALKPWNQPQI GAEWLLMGTG IGASNQFEAG
GFIRSDDSFE WPNIQYHFLP VAINYNGSNP IRVHSFQAHM GSMRSPSRGR IHLRSKDPRQ
HPSILFNYMS TEQDWQEFRN GIRITRDIIA QQALSAYAGR EISPGVQVQT DAELDAFVRQ
HAETAFHPSC SNAMGYDEMA VVDNQGRVHG MEGLRVVDAS IMPLITTGNL NAPTIMIAEK
IADCIRGRQP LARLEVPYYV AGGKPARQG
//
