ID   LCDH_BURPS              Reviewed;         321 AA.
AC   Q63MT0;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=L-carnitine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02129};
DE            Short=CDH {ECO:0000255|HAMAP-Rule:MF_02129};
DE            Short=L-CDH {ECO:0000255|HAMAP-Rule:MF_02129};
DE            EC=1.1.1.108 {ECO:0000255|HAMAP-Rule:MF_02129};
GN   Name=lcdH {ECO:0000255|HAMAP-Rule:MF_02129}; OrderedLocusNames=BPSS0568;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-
CC       dehydrocarnitine. {ECO:0000255|HAMAP-Rule:MF_02129}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carnitine + NAD(+) = 3-dehydrocarnitine + H(+) + NADH;
CC         Xref=Rhea:RHEA:19265, ChEBI:CHEBI:15378, ChEBI:CHEBI:17126,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57885, ChEBI:CHEBI:57945;
CC         EC=1.1.1.108; Evidence={ECO:0000255|HAMAP-Rule:MF_02129};
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_02129}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02129}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02129}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. L-
CC       carnitine dehydrogenase subfamily. {ECO:0000255|HAMAP-Rule:MF_02129}.
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DR   EMBL; BX571966; CAH38025.1; -; Genomic_DNA.
DR   RefSeq; WP_009923734.1; NZ_CP009537.1.
DR   RefSeq; YP_110589.1; NC_006351.1.
DR   AlphaFoldDB; Q63MT0; -.
DR   SMR; Q63MT0; -.
DR   STRING; 272560.BPSS0568; -.
DR   PRIDE; Q63MT0; -.
DR   EnsemblBacteria; CAH38025; CAH38025; BPSS0568.
DR   KEGG; bps:BPSS0568; -.
DR   PATRIC; fig|272560.51.peg.6737; -.
DR   eggNOG; COG1250; Bacteria.
DR   OMA; KREIQGF; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000000605; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047728; F:carnitine 3-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0042413; P:carnitine catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   HAMAP; MF_02129; L_carnitine_dehydrog; 1.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR026578; L-carnitine_dehydrogenase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..321
FT                   /note="L-carnitine dehydrogenase"
FT                   /id="PRO_0000417898"
FT   BINDING         14..19
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02129"
SQ   SEQUENCE   321 AA;  34839 MW;  C8B924499DA56E8D CRC64;
     MAVITKIDTF AAIGAGVIGS GWVARALANG LDVLAWDPAE GAEMQLRANV ENAWPALERA
     GLAPGASPAR LHFVPTIEAC VADADFVQES APEREALKLE LHERISRAAK PDAIIASSTS
     GLLPTDFYAR AHRPERCIVG HPFNPVYLLP LVEVLGGERT APDTVDAALG IYRALGMRPL
     RVRKEVPGFI ADRLLEALWR EALHLVDEGV ATTGEIDDAI RFGAGIRWSF MGTFLTYTLA
     GGEAGMRHFM QQFGPALELP WTKLVAPKLT DALIDRVVEG TAEQQGPRSI KALERYRDEC
     ITEVIAAIAA VKARHGMRYE D