LCDH_PSEAE
ID LCDH_PSEAE Reviewed; 321 AA.
AC Q9HTH8;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=L-carnitine dehydrogenase;
DE Short=CDH;
DE Short=L-CDH;
DE EC=1.1.1.108;
GN Name=lcdH; Synonyms=cdhA; OrderedLocusNames=PA5386;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=NCTC A7244;
RX PubMed=4302217; DOI=10.1111/j.1432-1033.1968.tb00437.x;
RA Aurich H., Kleber H.P., Sorger H., Tauchert H.;
RT "Purification and properties of carnitine dehydrogenase from Pseudomonas
RT aeruginosa.";
RL Eur. J. Biochem. 6:196-201(1968).
RN [3]
RP FUNCTION IN CARNITINE CATABOLISM, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=19406895; DOI=10.1099/mic.0.028787-0;
RA Wargo M.J., Hogan D.A.;
RT "Identification of genes required for Pseudomonas aeruginosa carnitine
RT catabolism.";
RL Microbiology 155:2411-2419(2009).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-
CC dehydrocarnitine. Is specific for L-carnitine and NAD(+) as substrates.
CC D,L-3-hydroxybutyrate, L-lactate, ethanol, L-malate and D,L-isocitrate
CC are not substrates. Is involved in a L-carnitine degradation pathway
CC that allows P.aeruginosa to grow on L-carnitine as the sole source of
CC carbon and nitrogen. {ECO:0000269|PubMed:19406895,
CC ECO:0000269|PubMed:4302217}.
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:4302217};
CC -!- ACTIVITY REGULATION: Analogs of L-carnitine such as D-carnitine,
CC glycine betaine and choline, are competitive inhibitors of L-carnitine
CC oxidation. {ECO:0000269|PubMed:4302217}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26 mM for L-carnitine (at pH 9.5) {ECO:0000269|PubMed:4302217};
CC KM=8.9 mM for L-carnitine (at pH 9.0) {ECO:0000269|PubMed:4302217};
CC KM=0.16 mM for NAD(+) (at pH 9.0) {ECO:0000269|PubMed:4302217};
CC KM=1.3 mM for 3-dehydrocarnitine (at pH 7.2)
CC {ECO:0000269|PubMed:4302217};
CC KM=0.022 mM for NADH (at pH 7.2) {ECO:0000269|PubMed:4302217};
CC pH dependence:
CC Optimum pH is 9-9.5 for the forward reaction (oxidation) and 7.0 for
CC the reverse reaction (reduction). {ECO:0000269|PubMed:4302217};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius for the reaction in both
CC directions. {ECO:0000269|PubMed:4302217};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Highly induced by carnitine via the CdhR transcriptional
CC regulator. Not induced by glycine betaine or pyruvate.
CC {ECO:0000269|PubMed:19406895}.
CC -!- DISRUPTION PHENOTYPE: Cells are incapable of growth on carnitine.
CC {ECO:0000269|PubMed:19406895}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. L-
CC carnitine dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; AE004091; AAG08771.1; -; Genomic_DNA.
DR PIR; F82972; F82972.
DR RefSeq; NP_254073.1; NC_002516.2.
DR RefSeq; WP_003096713.1; NZ_QZGE01000031.1.
DR AlphaFoldDB; Q9HTH8; -.
DR SMR; Q9HTH8; -.
DR STRING; 287.DR97_2762; -.
DR PaxDb; Q9HTH8; -.
DR EnsemblBacteria; AAG08771; AAG08771; PA5386.
DR GeneID; 881645; -.
DR KEGG; pae:PA5386; -.
DR PATRIC; fig|208964.12.peg.5646; -.
DR PseudoCAP; PA5386; -.
DR HOGENOM; CLU_009834_0_1_6; -.
DR InParanoid; Q9HTH8; -.
DR OMA; KREIQGF; -.
DR PhylomeDB; Q9HTH8; -.
DR BioCyc; MetaCyc:G1FZ6-5513-MON; -.
DR BioCyc; PAER208964:G1FZ6-5513-MON; -.
DR BRENDA; 1.1.1.108; 5087.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000002438; 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:0050104; F:L-gulonate 3-dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042413; P:carnitine catabolic process; IMP:PseudoCAP.
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; IPR022694; 3-OHacyl-CoA_DH.
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 PIRSF; PIRSF000105; HCDH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..321
FT /note="L-carnitine dehydrogenase"
FT /id="PRO_0000417901"
FT REGION 317..321
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT BINDING 14..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 321 AA; 34695 MW; C7FDBA55F8EECA07 CRC64;
MSFVTEIKTF AALGSGVIGS GWIARALAHG LDVVAWDPAP GAEAALRARV ANAWPALRKQ
GLAPGAAQER LRFVASIEEC VGDADFIQES APERLDLKLD LHARISAAAR PDVLIGSSTS
GLLPSEFYAE ASHPERCLVG HPFNPVYLLP LVEVVGGERT AAEAVRAAMR VYESLGMRPL
HVRKEVPGFI ADRLLEALWR EALHLVNDGV ATTGEIDDAI RFGAGLRWSF MGTFLTYTLA
GGNAGMRHFM AQFGPALQLP WTYLPAPELT EALIDRVVEG TAEQQGARSI AELERYRDDC
LLAVLGAIRE TKARHGFAFA E
