ID   LCDH_BURMA              Reviewed;         321 AA.
AC   Q62DG4;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 2.
DT   03-AUG-2022, entry version 96.
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=BMAA0492;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU46625.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; CP000011; AAU46625.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_024900416.1; NC_006349.2.
DR   RefSeq; YP_105264.1; NC_006349.2.
DR   AlphaFoldDB; Q62DG4; -.
DR   SMR; Q62DG4; -.
DR   STRING; 243160.BMAA0492; -.
DR   EnsemblBacteria; AAU46625; AAU46625; BMAA0492.
DR   KEGG; bma:BMAA0492; -.
DR   PATRIC; fig|243160.12.peg.3998; -.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_0_1_4; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000006693; 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.
FT   CHAIN           1..321
FT                   /note="L-carnitine dehydrogenase"
FT                   /id="PRO_0000417897"
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;  34897 MW;  C87AD8769C68725D CRC64;
     MAVITKIDTF AAIGAGVIGS GWVARALANG LDVLAWDPAE DAEMQLRANV 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