ID A0A0P1FAM0_9RHOB Unreviewed; 491 AA.
AC A0A0P1FAM0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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_2 {ECO:0000313|EMBL:CUH53205.1};
GN Synonyms=lcdH {ECO:0000256|HAMAP-Rule:MF_02129};
GN ORFNames=SHM7688_02657 {ECO:0000313|EMBL:CUH53205.1};
OS Shimia marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=321267 {ECO:0000313|EMBL:CUH53205.1, ECO:0000313|Proteomes:UP000054823};
RN [1] {ECO:0000313|EMBL:CUH53205.1, ECO:0000313|Proteomes:UP000054823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7688 {ECO:0000313|EMBL:CUH53205.1,
RC ECO:0000313|Proteomes:UP000054823};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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; CYPW01000027; CUH53205.1; -; Genomic_DNA.
DR RefSeq; WP_058240384.1; NZ_FOMU01000002.1.
DR AlphaFoldDB; A0A0P1FAM0; -.
DR STRING; 321267.SHM7688_02657; -.
DR OrthoDB; 9803287at2; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000054823; 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 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:CUH53205.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054823}.
FT DOMAIN 5..179
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 185..251
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT BINDING 9..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02129"
SQ SEQUENCE 491 AA; 54288 MW; 29CAA5E173636C6F CRC64;
MTKTAAIIGG GVIGGGWAAR FLLNGWDVRV FDPDPEAERK IGEVIANARV SLPGLSDTAL
PAEGALSFHE TMSEAVHGAA WIQESVPERL ELKRKVYQTL QEHCAEDAII GSSTSGFKPS
ELQGCASRPE QIVVTHPFNP VYLMPLIEVV PTEKNPPEMV ARVKEILTGV GMFPLHVRKE
IDAHIADRFL EAVWREALWL VKDGIATTEE IDEAIRMGFG IRWAQMGLFD TYRVAGGEAG
MKHFMAQFGP ALEWPWTKLM DVPEFTEELV DLIAGQSDAQ SGHMSIREME RIRDNNLVAM
MRALKAQDFA SGAVLNQHDA KLSAEAGMVR TAREIADPSQ PIVTVRRAVP IDWLDYNGHM
TESRYLHAFA DATDRLMEII GCDQAYIATG GSFFTAETHI RHIDETHLGS VIEVHTRVLM
GEGKKMHVFH EMYAGEKLLA TGEHILIHVS LETRRPAPFS EEIAANLKMI CEAQAKLPAP
EGAGRYVGQP R
//
