ID   LCDH_AGRFC              Reviewed;         484 AA.
AC   Q7D3B2;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=L-carnitine dehydrogenase;
DE            Short=CDH;
DE            Short=L-CDH;
DE            EC=1.1.1.108;
GN   Name=lcdH; OrderedLocusNames=Atu5344;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OG   Plasmid AT.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
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}.
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DR   EMBL; AE007872; AAK90717.2; -; Genomic_DNA.
DR   RefSeq; NP_396276.2; NC_003064.2.
DR   RefSeq; WP_010974598.1; NC_003064.2.
DR   AlphaFoldDB; Q7D3B2; -.
DR   SMR; Q7D3B2; -.
DR   STRING; 176299.Atu5344; -.
DR   EnsemblBacteria; AAK90717; AAK90717; Atu5344.
DR   KEGG; atu:Atu5344; -.
DR   PATRIC; fig|176299.10.peg.5016; -.
DR   eggNOG; COG0824; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_578448_0_0_5; -.
DR   OMA; TDYNGHM; -.
DR   PhylomeDB; Q7D3B2; -.
DR   BioCyc; AGRO:ATU5344-MON; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000000813; Plasmid At.
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; Plasmid; Reference proteome.
FT   CHAIN           1..484
FT                   /note="L-carnitine dehydrogenase"
FT                   /id="PRO_0000417895"
FT   REGION          1..322
FT                   /note="L-carnitine dehydrogenase"
FT   REGION          323..484
FT                   /note="Unknown"
FT   BINDING         7..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   484 AA;  53035 MW;  6ABECBF52052AC99 CRC64;
     MKIAAIGGGV IGGGWIARFI LAGHDVTVFD PHPEANRIVT EVMANAAEAW GRLYQSPLPK
     PGSINWASSI AEAVAGADYI QESVPERLDL KHRIIAEIEA TASPQAIIAS STSGFKPSEL
     REGSVHSERV IVAHPFNPVY LLPVVEVVGG GVAAQRASDI LVSVGMKPVQ IGREIDAHIG
     DRLLEAIWRE ALWLVKDGIA TTQEIDDIIR YGFGLRWAQM GLFETYRIAG GEAGMRHFLA
     QFGPALKWPW TKLMDVPEFN DELIDLIAGQ SDAQSGAYSI RELERIRDSN LIGIFHALKA
     NDWGAGQTVK AMENRFYARN GKVQADYPLR LHEAHVNGGW VDYNGHMTEF RYLQVLGDAT
     DALLIHIGLD ADYRAAGHSA YTVETHIRHL AEVKAGARLT VETRLLGYDD KRLRLHHAIL
     NEDGETVATG EHMLLHVDTK ANRTVAMPPA LMRALDHLNA QEEGPLPDHA GSGIRAVRLK
     ETSA