LCDH_RHIME
ID LCDH_RHIME Reviewed; 496 AA.
AC Q92NF5;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=L-carnitine dehydrogenase;
DE Short=CDH;
DE Short=L-CDH;
DE EC=1.1.1.108;
GN Name=lcdH; OrderedLocusNames=R02250; ORFNames=SMc01638;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-
CC dehydrocarnitine. {ECO:0000250}.
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;
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. L-carnitine dehydrogenase subfamily.
CC {ECO:0000305}.
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DR EMBL; AL591688; CAC46829.1; -; Genomic_DNA.
DR RefSeq; NP_386356.1; NC_003047.1.
DR RefSeq; WP_003537893.1; NC_003047.1.
DR AlphaFoldDB; Q92NF5; -.
DR SMR; Q92NF5; -.
DR STRING; 266834.SMc01638; -.
DR EnsemblBacteria; CAC46829; CAC46829; SMc01638.
DR GeneID; 61603714; -.
DR KEGG; sme:SMc01638; -.
DR PATRIC; fig|266834.11.peg.3719; -.
DR eggNOG; COG0824; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_578448_0_0_5; -.
DR OMA; KREIQGF; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000001976; 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; 1.10.1040.10; -; 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 Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..496
FT /note="L-carnitine dehydrogenase"
FT /id="PRO_0000417905"
FT REGION 1..335
FT /note="L-carnitine dehydrogenase"
FT REGION 336..496
FT /note="Unknown"
FT BINDING 11..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 496 AA; 54306 MW; 1224CB171110F187 CRC64;
MTTITKAACI GGGVIGGAWA ARFALAGIDV NIFDPHPEAE RIIGEVMANA ERAYGMLTMA
PLPPRGKFTF CRSIQEAVEG VDWIQESVPE RLPLKRGVIN EIDAAARPDA LIGSSTSGLL
PSDLQAEMKH PERMFVAHPY NPVYLLPLVE LVGGRKTSPE TIRRAEEAVA EIGMKGVVIA
KEIEAFVGDR LLEALWREAL WLIQDDICDT ETLDDVMRYS FGMRWAQMGL FETYRIAGGE
AGMRHFLAQF GPCLKWPWTK FTDVVDLDDA LVEKIGAQSD AQAAGRSIRE LERIRDENLV
GIMHALKAGD GGKGWGAGKL LADFEKRLWE KGGSPSKSLD ASGPLRLVDT KVNAAWVDYN
GHMTEHRYLQ LFGDTSDALL KVIGVDFAYV EAGHSYYTVE THIRHLGEAK LGQALYTTLQ
LLSSDEKRIH FFTRIHDAAS GDVIATAEQM MLHVDAKAGK SVPAPAEVMA KLKPIAEGHA
KLDAPDGAGR HVGQKR
