ID A0A0B4REL6_9BACL Unreviewed; 320 AA.
AC A0A0B4REL6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=L-carnitine dehydrogenase {ECO:0000256|ARBA:ARBA00021240, ECO:0000256|HAMAP-Rule:MF_02129};
DE Short=CDH {ECO:0000256|HAMAP-Rule:MF_02129};
DE Short=L-CDH {ECO:0000256|HAMAP-Rule:MF_02129};
DE EC=1.1.1.108 {ECO:0000256|ARBA:ARBA00012956, ECO:0000256|HAMAP-Rule:MF_02129};
GN Name=lcdH {ECO:0000256|HAMAP-Rule:MF_02129};
GN ORFNames=Plano_2658 {ECO:0000313|EMBL:AIY06623.1};
OS Planococcus sp. PAMC 21323.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1526927 {ECO:0000313|EMBL:AIY06623.1, ECO:0000313|Proteomes:UP000031496};
RN [1] {ECO:0000313|EMBL:AIY06623.1, ECO:0000313|Proteomes:UP000031496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 21323 {ECO:0000313|EMBL:AIY06623.1,
RC ECO:0000313|Proteomes:UP000031496};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-i.;
RT "Complete genome sequence of Planococcus sp. PAMC21323 isolated from the
RT Antarctica.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-
CC dehydrocarnitine. {ECO:0000256|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:0000256|ARBA:ARBA00001215,
CC ECO:0000256|HAMAP-Rule:MF_02129};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000256|ARBA:ARBA00004855, ECO:0000256|HAMAP-Rule:MF_02129}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_02129}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_02129}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. L-
CC carnitine dehydrogenase subfamily. {ECO:0000256|HAMAP-Rule:MF_02129}.
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DR EMBL; CP009129; AIY06623.1; -; Genomic_DNA.
DR RefSeq; WP_038704956.1; NZ_CP009129.1.
DR AlphaFoldDB; A0A0B4REL6; -.
DR STRING; 1526927.Plano_2658; -.
DR KEGG; pln:Plano_2658; -.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_0_1_9; -.
DR OrthoDB; 9815331at2; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000031496; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF1; LAMBDA-CRYSTALLIN HOMOLOG; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02129};
KW NAD {ECO:0000256|HAMAP-Rule:MF_02129};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02129};
KW Reference proteome {ECO:0000313|Proteomes:UP000031496}.
FT DOMAIN 10..185
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 189..269
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT BINDING 15..20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02129"
SQ SEQUENCE 320 AA; 35225 MW; 6512392E8FE6EBB7 CRC64;
MSEHVSQFKK VAVVGTGVIG NGWIARFLAQ GFDVIAFDPA EGAQERTQKA LDQAWPSLEK
IGLAEGADRN RLTFMPTIEE AVSDADLIQE NVPEREDLKK SVLASIDTYA KVDAIIGSST
SGIMPSVLQE GLKHPERLIV AHPFNPVYIL PLVELVAGSK TDANIVERAK NFYASVGMKP
LIIQKEIEGH LADRLMEALW REALHLVNDG VATTEEVDAA IIYGAGLRWA QMGPFLTFHL
AGGEKGMRHM LEQFGPALKL PWTKLEAPEL TDELKEKVIT GCESHANDST IAELENKRNE
FLVELLDLVE SYWPETTAAK
//
