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LCDH_OCEIH
ID   LCDH_OCEIH              Reviewed;         307 AA.
AC   Q8CUW0;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=OB0997;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC12953.1; -; Genomic_DNA.
DR   RefSeq; WP_011065400.1; NC_004193.1.
DR   AlphaFoldDB; Q8CUW0; -.
DR   SMR; Q8CUW0; -.
DR   STRING; 221109.22776678; -.
DR   EnsemblBacteria; BAC12953; BAC12953; BAC12953.
DR   KEGG; oih:OB0997; -.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_0_1_9; -.
DR   OMA; RDNCLTH; -.
DR   OrthoDB; 862072at2; -.
DR   PhylomeDB; Q8CUW0; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000000822; 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; Reference proteome.
FT   CHAIN           1..307
FT                   /note="L-carnitine dehydrogenase"
FT                   /id="PRO_0000417900"
FT   BINDING         8..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02129"
SQ   SEQUENCE   307 AA;  34183 MW;  E4B6186EB33E3A0B CRC64;
     MKKVAVIGTG VIGNGWITRF LANGCEVVAH DPAPGAKERT IQAIENAWES VEQLGLKEGA
     SKDSLTFVDS IEEAVKDADL IQESVPERYE LKHGVLKEID RFAHSNTIIG SSTSGIKPTD
     LQIGLNHPER LVVAHPFNPV YLLPLVEIVG GEATTKEITN RASVYYESLQ MKPMVIEKEI
     EGFVADRLME ALWREALHLV NDGIATTEEV DKAITYGAGL RWAQMGPFMT FHLAGGNAGM
     RHMLEQFGPA LKLPWTKLEA PELTDELKER VIQGCETHAN DRSVEELEKK RNEFLVKLID
     LVEDYWP
 
 
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