ID   LCDH_RUEPO              Reviewed;         487 AA.
AC   Q5LTH8;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=L-carnitine dehydrogenase;
DE            Short=CDH;
DE            Short=L-CDH;
DE            EC=1.1.1.108;
GN   Name=lcdH; OrderedLocusNames=SPO1436;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-
CC       dehydrocarnitine. {ECO:0000250}.
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;
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. L-carnitine dehydrogenase subfamily.
CC       {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; CP000031; AAV94723.1; -; Genomic_DNA.
DR   RefSeq; WP_011047173.1; NC_003911.12.
DR   AlphaFoldDB; Q5LTH8; -.
DR   SMR; Q5LTH8; -.
DR   STRING; 246200.SPO1436; -.
DR   EnsemblBacteria; AAV94723; AAV94723; SPO1436.
DR   KEGG; sil:SPO1436; -.
DR   eggNOG; COG0824; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_578448_0_0_5; -.
DR   OMA; TDYNGHM; -.
DR   OrthoDB; 478797at2; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001023; 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; IPR029069; HotDog_dom_sf.
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.
DR   SUPFAM; SSF54637; SSF54637; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..487
FT                   /note="L-carnitine dehydrogenase"
FT                   /id="PRO_0000417907"
FT   REGION          1..327
FT                   /note="L-carnitine dehydrogenase"
FT   REGION          328..487
FT                   /note="Unknown"
FT   BINDING         8..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   487 AA;  53505 MW;  C414A8B46367A135 CRC64;
     MTTAAIIGGG VIGGGWAARF LLNGWDVRVF DPDPEAERKI GEVLANARRS LPGLSDMPLP
     PEGKLSFHAD LGEAVTGAAW IQESVPERLD LKLKVYRSIQ EACDPGAILG SSTSGFKPSE
     LQEGALRPGQ IVVTHPFNPV YLLPLIELVT TPENSPEMIE RAKEIMRGLG QFPLHVRKEI
     DAHIADRFLE AVWREALWLV KDGIATTEEI DEAIRMGFGI RWAQMGLFET YRVAGGEAGM
     KHFMAQFGPC LSWPWTKLMD VPEFTDELVD LIAGQSDAQS GHHTIRELER IRDNNLVGMM
     RALKAQNWGA GAVLNKHDAA LKPKALPDLD TADLTQPILT LSRAVPLDWT DYNGHMTESK
     YLEAFANSTD RFMEIIGCDA DYIAAGGSYF TAETHIRHLD EAHAGARIRV ETQMLLGQGK
     KLHLFHRMYE GDKLLATGES FLLHVSLETR KPCAPSPEIE AAMARIAEAQ AGLSYPEGAG
     SAIRKPA