ID   LCDH_STAES              Reviewed;         321 AA.
AC   Q8CQB9;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=SE_0220;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO03817.1; -; Genomic_DNA.
DR   RefSeq; NP_763775.1; NC_004461.1.
DR   RefSeq; WP_001830516.1; NZ_WBME01000011.1.
DR   AlphaFoldDB; Q8CQB9; -.
DR   SMR; Q8CQB9; -.
DR   STRING; 176280.SE_0220; -.
DR   PRIDE; Q8CQB9; -.
DR   EnsemblBacteria; AAO03817; AAO03817; SE_0220.
DR   GeneID; 50017616; -.
DR   KEGG; sep:SE_0220; -.
DR   PATRIC; fig|176280.10.peg.199; -.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_0_1_9; -.
DR   OMA; RDNCLTH; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001411; Chromosome.
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_0000417908"
FT   BINDING         7..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02129"
SQ   SEQUENCE   321 AA;  35774 MW;  5B71ECADA18D45AC CRC64;
     MKFAVVGTGV IGSGWITRML AHGHEVIATD PSEGAYERML TQVKQNWPYA EQMGLAENAS
     IQNLTFTPHL EEAVKDADHI QENVPEVEEI KDAVLKEIDF YAKPEATIGS STSGIMPSEL
     QANLSHPERL VVAHPFHPVY ILPLVEIVPG KQTSEETTVK AEQIYESIGM DVLHVRHEIE
     GHIADRLMEA LWRESLHIVN DGIATTEEVD KAFTHAAGLR YAQYGPFMTF HLAGGEGGMR
     HMLKQFGPAL KKPWTKLIAP ELTDDLYHKV VSGSEASSQG YTMSELDQKR NEFLIKVKEL
     AEQYWPSDSK AMKKSNGAEL Q