LCDH_PSESP
ID LCDH_PSESP Reviewed; 321 AA.
AC D7URM0;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=L-carnitine dehydrogenase;
DE Short=CDH;
DE Short=L-CDH;
DE EC=1.1.1.108;
GN Name=lcdH; Synonyms=Xt-cdh;
OS Pseudomonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 317-MET--GLU-321.
RC STRAIN=NBRC 13558;
RX PubMed=20530902; DOI=10.1271/bbb.100072;
RA Arima J., Uesumi A., Mitsuzumi H., Mori N.;
RT "Biochemical characterization of L-carnitine dehydrogenases from Rhizobium
RT sp. and Xanthomonas translucens.";
RL Biosci. Biotechnol. Biochem. 74:1237-1242(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=NBRC 13558;
RA Mori N., Kasugai T., Kitamoto Y., Ichikawa Y.;
RT "Purification and some properties of carnitine dehydrogenase from
RT Xanthomonas translucens.";
RL Agric. Biol. Chem. 52:249-250(1988).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-
CC dehydrocarnitine. Is specific for L-carnitine and NAD(+) as substrates
CC since D-carnitine, other carnitine analogs such as choline and betaine,
CC and NADP(+) are not substrates. Despite a high similarity to 3-
CC hydroxyacyl-CoA dehydrogenases, cannot dehydrogenate 3-hydroxybutylate
CC and 3-hydroxybutyl-CoA. Is probably involved in a L-carnitine
CC degradation pathway that allows Xanthomonas translucens to grow on L-
CC carnitine as the sole source of carbon and nitrogen.
CC {ECO:0000269|PubMed:20530902, ECO:0000269|Ref.2}.
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:0000269|PubMed:20530902,
CC ECO:0000269|Ref.2};
CC -!- ACTIVITY REGULATION: The enzyme activity is strongly inhibited by
CC Ag(+), Ni(+), Hg(+), and p-chloromercuribenzoate, and partially
CC inhibited by Li(+), Ca(2+), Mn(2+), Co(2+), Cu(2+), and Zn(2+).
CC {ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 mM for L-carnithine {ECO:0000269|Ref.2};
CC KM=8.5 mM for L-carnithine {ECO:0000269|PubMed:20530902};
CC KM=0.25 mM for NAD(+) {ECO:0000269|Ref.2};
CC KM=0.24 mM for NAD(+) {ECO:0000269|PubMed:20530902};
CC KM=1.71 mM for 3-dehydrocarnitine {ECO:0000269|Ref.2};
CC KM=4.5 mM for 3-dehydrocarnitine {ECO:0000269|PubMed:20530902};
CC KM=0.04 mM for NADH {ECO:0000269|Ref.2};
CC Vmax=21.9 umol/min/mg enzyme {ECO:0000269|PubMed:20530902};
CC Note=Part of the values are for the recombinant protein expressed in
CC E.coli (PubMed:20530902). Other values are for the wild-type protein
CC (Ref.2).;
CC pH dependence:
CC Optimum pH is 9.5 for the oxidation reaction and 6.5 for the
CC reduction reaction. {ECO:0000269|Ref.2};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20530902}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. L-
CC carnitine dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; AB537424; BAJ10560.1; -; Genomic_DNA.
DR AlphaFoldDB; D7URM0; -.
DR SMR; D7URM0; -.
DR SABIO-RK; D7URM0; -.
DR UniPathway; UPA00117; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0047728; F:carnitine 3-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0042413; P:carnitine catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase.
FT CHAIN 1..321
FT /note="L-carnitine dehydrogenase"
FT /id="PRO_0000417911"
FT REGION 317..321
FT /note="Important for catalytic activity"
FT BINDING 14..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MUTAGEN 317..321
FT /note="Missing: Marked decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:20530902"
SQ SEQUENCE 321 AA; 34755 MW; 822871104109A9C5 CRC64;
MPFITHIKTF AALGSGVIGS GWVARALAHG LDVIAWDPAP GAEQALRQRV ANAWPALEKQ
GLAAGAAQHR LSFVSSIEEC VRDADFIQES APERLDLKLD LHAKISAAAK PDAIIASSTS
GLLPSEFYES SSHPERCVVG HPFNPVYLLP LVEIVGGRHT APEAIEAAKG IYTELGMRPL
HVRKEVPGFI ADRLLEALWR EALHLVNDGV ATTGEIDDAI RFGAGLRWSF MGTFLTYTLA
GGDAGMRHFM QQFGPALKLP WTYLPAPELT ERLIDEVVDG TAAQVGERSI AELERYRDDT
LLAVLEAIGT SKAKHGMTFS E
