ID A0A418SD76_9RHOB Unreviewed; 499 AA.
AC A0A418SD76;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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_1 {ECO:0000313|EMBL:QPM92284.1};
GN Synonyms=lcdH {ECO:0000256|HAMAP-Rule:MF_02129};
GN ORFNames=PSAL_035480 {ECO:0000313|EMBL:QPM92284.1};
OS Pseudooceanicola algae.
OG Plasmid p202 {ECO:0000313|EMBL:QPM92284.1,
OG ECO:0000313|Proteomes:UP000283786}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1537215 {ECO:0000313|EMBL:QPM92284.1, ECO:0000313|Proteomes:UP000283786};
RN [1] {ECO:0000313|EMBL:QPM92284.1, ECO:0000313|Proteomes:UP000283786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lw-13e {ECO:0000313|EMBL:QPM92284.1,
RC ECO:0000313|Proteomes:UP000283786};
RC PLASMID=p202 {ECO:0000313|EMBL:QPM92284.1,
RC ECO:0000313|Proteomes:UP000283786};
RA Poehlein A., Wolter L., Daniel R., Brinkhoff T.;
RT "Genome sequence of Rhodobacteraceae bacterium Lw-13e.";
RL Submitted (AUG-2020) 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; CP060437; QPM92284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418SD76; -.
DR KEGG; palw:PSAL_035480; -.
DR OrthoDB; 9803287at2; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000283786; Plasmid p202.
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 CDD; cd00586; 4HBT; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
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; IPR029069; HotDog_dom_sf.
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 Pfam; PF13279; 4HBT_2; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 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 ECO:0000313|EMBL:QPM92284.1}; Plasmid {ECO:0000313|EMBL:QPM92284.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000283786}.
FT DOMAIN 7..182
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 188..254
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT BINDING 12..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02129"
SQ SEQUENCE 499 AA; 55299 MW; 0B939AC85B75F4B4 CRC64;
MSRIIQKAAC VGGGVIGGGW IARFLLNGID VAVHDPHPEA RRIVGEVLDN ARHAYRAMMN
APLGPEGALT FHDDLAEAVA DAEYIQESVP ERLDLKHRVF AAIEAAARPD ALIGSSTSGF
KPSELQVGMA HPERLFVAHP FNPVYLVPLV EVVGSPVNDE AALSRAMEIQ RETGLHPLRV
RKEIDAHIGD RLLEAVWRES LWLVHDDVAT TQEIDDVIRF SFGLRWAQMG LFETYRIAGG
EAGMKHFIEQ FGPALKWPWT KLMDVPEMTD DLATKIGDQS DAQSGMHSIR ELERIRDDNL
VGIYQALKAN DWGAGKTLRE MEDRFFERAK DSAAAAAPDY AAPLVLHETR VPGDWLDYNG
HMTEYRYLQV FGDATDAFLG HIGMDAAYRA PGRSVYTVES HIRHLAETSV DTRLCVRTCV
LGHDARRIRL HHEMVDEAGN VQATSEHMLM HVDTNAGKAS PLEAPLTDRL ARLSRGQRGL
TAPAHAGRPI RDIGWPEPV
//
