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Database: UniProt
Entry: D0SDY8_ACIJO
LinkDB: D0SDY8_ACIJO
Original site: D0SDY8_ACIJO 
ID   D0SDY8_ACIJO            Unreviewed;       571 AA.
AC   D0SDY8;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
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:EEY95648.1};
GN   ORFNames=HMPREF0016_02061 {ECO:0000313|EMBL:EEY95648.1};
OS   Acinetobacter johnsonii SH046.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=575586 {ECO:0000313|EMBL:EEY95648.1, ECO:0000313|Proteomes:UP000012047};
RN   [1] {ECO:0000313|Proteomes:UP000012047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH046 {ECO:0000313|Proteomes:UP000012047};
RX   PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA   Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA   Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA   Seifert H., Dijkshoorn L.;
RT   "The success of Acinetobacter species; genetic, metabolic and
RT   virulence attributes.";
RL   PLoS ONE 7:E46984-E46984(2012).
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|HAMAP-Rule:MF_00750, 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|HAMAP-Rule:MF_00750,
CC         ECO:0000256|RuleBase:RU003969, 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|HAMAP-Rule:MF_00750,
CC         ECO:0000256|SAAS:SAAS01117337};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00750, 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|HAMAP-Rule:MF_00750,
CC       ECO:0000256|RuleBase:RU003969, ECO:0000256|SAAS:SAAS00321105}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00750, ECO:0000256|RuleBase:RU003968,
CC       ECO:0000256|SAAS:SAAS01080758}.
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DR   EMBL; GG704967; EEY95648.1; -; Genomic_DNA.
DR   STRING; 575586.HMPREF0016_02061; -.
DR   EnsemblBacteria; EEY95648; EEY95648; HMPREF0016_02061.
DR   eggNOG; ENOG4105CZ6; Bacteria.
DR   eggNOG; COG2303; LUCA.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000012047; 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-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; -; 1.
DR   Gene3D; 4.10.450.10; -; 1.
DR   HAMAP; MF_00750; Choline_dehydrogen; 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   PANTHER; PTHR11552:SF157; PTHR11552:SF157; 1.
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:UP000012047};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_00750, ECO:0000256|RuleBase:RU003968,
KW   ECO:0000256|SAAS:SAAS01080750};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00750,
KW   ECO:0000256|RuleBase:RU003968, ECO:0000256|SAAS:SAAS01080744};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00750, ECO:0000256|SAAS:SAAS00321145};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00750,
KW   ECO:0000256|SAAS:SAAS01080751, ECO:0000313|EMBL:EEY95648.1}.
FT   DOMAIN      102    125       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00623}.
FT   DOMAIN      280    294       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00624}.
FT   NP_BIND      24     53       FAD. {ECO:0000256|HAMAP-Rule:MF_00750}.
FT   ACT_SITE    494    494       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00750}.
SQ   SEQUENCE   571 AA;  63340 MW;  E142904B92522C39 CRC64;
     MWPRSHATWP CHRKRIIMHS QHYDYIIIGA GSAGNVLAAR LTEDPDVSVL LLEAGGPDYR
     LDFRTQMPAA LAYPLQGRRY NWAYLTDPEP HMNNRRMECG RGKGLGGSSL INGMCYIRGN
     AMDLEQWATL KGLEDWSYAD CLPYYKKAET RDIGGNDYHG DAGPVSVATP KADNNVLFHA
     MVEAGVQAGY PRTDDLNGYQ QEGFGPMDRT VTPKGRRSST ARGYLDMAKG RANLTIITHA
     MTNQILFNGK QAIGVEYIQG ANQNNLLQVY ANKEVLLCAG AIASPQILQR SGVGSSTLLQ
     SLDIPVVHDL PGVGENLQDH LEMYLQYKCK QPVSLYPALK WQNQPAIGAE WLFNGIGIGA
     SNQFEAGGFI RSSKEFAWPN IQYHFLPVAI NYNGSNAVKE HGFQAHVGSM RSPSRGRVQV
     TSKNPFDHPS ILFNYMSTEQ DWQEFRDAIR ITREIMNQPA LDPYRGEEIS PGKDVSTDAE
     LDEFVRNHAE TAYHPSCSCK MGEDDMAVVD GQGRVHGMQN LRVVDASIMP LIITGNLNAT
     TIMMAEKIAD QIRGHQALPR STAPFYRAEI A
//
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