ID I4NAY7_9PSED Unreviewed; 321 AA.
AC I4NAY7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=PMM47T1_01275 {ECO:0000313|EMBL:EIK98627.1};
OS Pseudomonas sp. M47T1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK98627.1, ECO:0000313|Proteomes:UP000004339};
RN [1] {ECO:0000313|EMBL:EIK98627.1, ECO:0000313|Proteomes:UP000004339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M47T1 {ECO:0000313|EMBL:EIK98627.1,
RC ECO:0000313|Proteomes:UP000004339};
RX PubMed=22887683; DOI=10.1128/JB.01116-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL J. Bacteriol. 194:4789-4790(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIK98627.1}.
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DR EMBL; AJWX01000001; EIK98627.1; -; Genomic_DNA.
DR RefSeq; WP_008365021.1; NZ_AJWX01000001.1.
DR AlphaFoldDB; I4NAY7; -.
DR STRING; 1179778.PMM47T1_01275; -.
DR PATRIC; fig|1179778.3.peg.261; -.
DR eggNOG; COG1250; Bacteria.
DR OrthoDB; 9803287at2; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000004339; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000004339}.
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; 34801 MW; ECABB3EFA8CFB71E CRC64;
MTFITEIKTF AALGSGVIGS GWVARALAHG LDVVAWDPAP GAEAALRRRV ANAWPALVEK
GLAPGASQER LQFVDTIEAC VRHADFIQES APERLDLKLD LHARISAAAK PDALIGSSTS
GLLPSEFYEG ATHPERCVVG HPFNPVYLLP LVEVVGGRQT APEAVQAAIK VYESLGMRPL
HVRKEVPGFI ADRLLEALWR EALHLVNDGV ATTGEIDDAI RFGAGLRWSF MGTFLTYTLA
GGDAGMRHFM SQFGPALKLP WTYLPAPQLT DKLIDDVVDG TREQLGTHSI SALERYRDDC
LLAVLEAVRA TKAKHGMEFS E
//
