ID   LCDH_RHISP              Reviewed;         497 AA.
AC   D7UNT2;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=L-carnitine dehydrogenase;
DE            Short=CDH;
DE            Short=L-CDH;
DE            EC=1.1.1.108;
GN   Name=lcdH; Synonyms=Rs-cdh;
OS   Rhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP   CATALYTIC ACTIVITY, KINETIC PARAMETERS, SUBSTRATE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=YS-240;
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).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-
CC       dehydrocarnitine. Despite a high similarity to 3-hydroxyacyl-CoA
CC       dehydrogenases, cannot dehydrogenate 3-hydroxybutylate and 3-
CC       hydroxybutyl-CoA. Is probably involved in a L-carnitine degradation
CC       pathway that allows Rhizobium sp. YS-240 to grow on L-carnitine as the
CC       sole source of carbon and nitrogen. {ECO:0000269|PubMed:20530902}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.1 mM for L-carnithine {ECO:0000269|PubMed:20530902};
CC         KM=0.087 mM for NAD(+) {ECO:0000269|PubMed:20530902};
CC         KM=1.2 mM for 3-dehydrocarnitine {ECO:0000269|PubMed:20530902};
CC         Vmax=18.9 umol/min/mg enzyme {ECO:0000269|PubMed:20530902};
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20530902}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. L-carnitine dehydrogenase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB079692; BAJ10559.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7UNT2; -.
DR   SMR; D7UNT2; -.
DR   BRENDA; 1.1.1.108; 5351.
DR   SABIO-RK; D7UNT2; -.
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; 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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN           1..497
FT                   /note="L-carnitine dehydrogenase"
FT                   /id="PRO_0000417906"
FT   REGION          1..335
FT                   /note="L-carnitine dehydrogenase"
FT   REGION          330..335
FT                   /note="Important for dehydrogenase activity"
FT   REGION          336..497
FT                   /note="Unknown"
FT   BINDING         11..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   497 AA;  54474 MW;  AB3A44C44623CF1F CRC64;
     MSFITKAACV GGGVIGGAWV ARFALAGIDV KIFDPHPEAE RIIGEVMANA ERAYAMLTMA
     PLPPKGKLTF CKSIEEAVEG ADWIQESVPE RLELKRGVIT KIDAAARPDA LIGSSTSGLL
     PSDLQSEMHH PERMFVAHPY NPVYLLPLVE LVGGKKTSKA TIERAMQGVE QIGMKGVVIA
     KEIEAFVGDR LLEALWREAL WLIQDDICHT ETLDNVMRYS FGMRWAQMGL FETYRIAGGE
     AGMRHFLAQF GPCLKWPWTK FTDVVDLDDA LVEKIGAQSD AQAAGRSIRE LERIRDENLV
     GIMHALKSGN GGEGWGAGKL LADFEAKLWA NARKPEADLG DVKPLRILDT KVSAAWVDYN
     GHMTEHRYLQ VFGDTSDGVL RLIGVDLDYV RDGHSYYTVE THIRNLGDEA SGEALYSTCQ
     ILSSDEKRLH IFSTIYNAAT NEAVATAEQM MLHVDSKAGK AVAAPEAVLS KLRAITEAHA
     QLQTPDGAGR FVGQKRA