ID   LCDH_PSEU2              Reviewed;         318 AA.
AC   Q4ZSC0;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, 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=Psyr_2918;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY37952.1; -; Genomic_DNA.
DR   RefSeq; WP_011268084.1; NC_007005.1.
DR   RefSeq; YP_235990.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZSC0; -.
DR   SMR; Q4ZSC0; -.
DR   STRING; 205918.Psyr_2918; -.
DR   EnsemblBacteria; AAY37952; AAY37952; Psyr_2918.
DR   KEGG; psb:Psyr_2918; -.
DR   PATRIC; fig|205918.7.peg.2977; -.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_0_1_6; -.
DR   OMA; KREIQGF; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000000426; 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..318
FT                   /note="L-carnitine dehydrogenase"
FT                   /id="PRO_0000417903"
FT   BINDING         14..19
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02129"
SQ   SEQUENCE   318 AA;  34339 MW;  1A993171E5EAC8E7 CRC64;
     MSFITEIKTF AALGSGVIGS GWVSRALAHG LDVVAWDPAP GAEAALRNRV AKCWGALEQQ
     GLVPGASQNR LRFVATVEEC VRDADFIQES APERLELKLD LHSRISAAAR SNVLIGSSTS
     GLLPSDVYES SAHPERCVVG HPFNPVYLLP LVEVVGGKNT APAAIQAAIK VYESLGMRPL
     HVRKEVPGFI ADRLLEALWR EALHLVNDGV ATTGEIDDAI RFGAGLRWSF MGTFLTYTLA
     GGEAGMRHFM TQFGPALQLP WTYLPAPELT DKLIDDVVDG TTDQLGKHSI SGLERYRDDC
     LLAVLEAVKT TKARHGMA