ID M4XNW4_9PSED Unreviewed; 321 AA.
AC M4XNW4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=H681_25115 {ECO:0000313|EMBL:AGI26890.1};
OS Pseudomonas sp. ATCC 13867.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1294143 {ECO:0000313|EMBL:AGI26890.1, ECO:0000313|Proteomes:UP000012082};
RN [1] {ECO:0000313|EMBL:AGI26890.1, ECO:0000313|Proteomes:UP000012082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13867 {ECO:0000313|EMBL:AGI26890.1,
RC ECO:0000313|Proteomes:UP000012082};
RX PubMed=23723394;
RA Ainala S.K., Somasundar A., Park S.;
RT "Complete genome sequence of Pseudomonas denitrificans ATCC 13867.";
RL Genome Announc. 1:E00257-E00213(2013).
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; CP004143; AGI26890.1; -; Genomic_DNA.
DR RefSeq; WP_015479734.1; NC_020829.1.
DR AlphaFoldDB; M4XNW4; -.
DR STRING; 1294143.H681_25115; -.
DR KEGG; pdr:H681_25115; -.
DR PATRIC; fig|1294143.3.peg.5109; -.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_0_1_6; -.
DR OrthoDB; 9803287at2; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000012082; 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|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02129}.
FT DOMAIN 11..184
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 188..256
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT BINDING 14..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02129"
SQ SEQUENCE 321 AA; 34536 MW; DDC22AD5EBAC0CE1 CRC64;
MSFITHIKTF AALGSGVIGS GWVARALAHG LDVIAWDPAP GAEAALRARI ANAWPALEKA
GLVPGASPDR LRFVATVEEC VRDADFIQES APERLDLKCE LHARISAAAK PNALIGSSTS
GLLPSEFYAD ATHPERCVVG HPFNPVYLLP LVEVVGGAKT APEAIQAAIQ VYESLGMRPL
HVRKEVPGFI ADRLLEALWR EALHLVNDGV ASTGEIDDAI RFGAGLRWSF MGTFLTYTLA
GGNAGMRHFM AQFGPALQLP WTYLPAPELT DTLIDRVVEG TAEQQGSRSI AELERYRDDC
LLAVLGAIRD TKSEHGFAFA D
//
