(data stored in SCRATCH zone)

SWISSPROT: D7A308_STAND

ID   D7A308_STAND            Unreviewed;       503 AA.
AC   D7A308;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 49.
DE   RecName: Full=L-carnitine dehydrogenase {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|HAMAP-Rule:MF_02129};
GN   Name=lcdH {ECO:0000256|HAMAP-Rule:MF_02129};
GN   OrderedLocusNames=Snov_0393 {ECO:0000313|EMBL:ADH87726.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87726.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87726.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-carnitine
CC       to 3-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|HAMAP-Rule:MF_02129};
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_02129}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02129}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02129}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       L-carnitine dehydrogenase subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_02129}.
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DR   EMBL; CP002026; ADH87726.1; -; Genomic_DNA.
DR   RefSeq; WP_013165231.1; NC_014217.1.
DR   STRING; 639283.Snov_0393; -.
DR   EnsemblBacteria; ADH87726; ADH87726; Snov_0393.
DR   KEGG; sno:Snov_0393; -.
DR   eggNOG; ENOG4105F35; Bacteria.
DR   eggNOG; COG0824; LUCA.
DR   eggNOG; COG1250; LUCA.
DR   HOGENOM; HOG000141499; -.
DR   KO; K17735; -.
DR   OMA; TDYNGHM; -.
DR   OrthoDB; 478797at2; -.
DR   BioCyc; SNOV639283:G1GLM-398-MONOMER; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000006633; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0047728; F:carnitine 3-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; D7A308.
DR   SWISS-2DPAGE; D7A308.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006633};
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   Reference proteome {ECO:0000313|Proteomes:UP000006633}.
FT   DOMAIN       10    182       3HCDH_N. {ECO:0000259|Pfam:PF02737}.
FT   DOMAIN      189    254       3HCDH. {ECO:0000259|Pfam:PF00725}.
FT   NP_BIND      14     19       NAD. {ECO:0000256|HAMAP-Rule:MF_02129}.
SQ   SEQUENCE   503 AA;  54472 MW;  83B2956C660C3818 CRC64;
     MTSLAPISRA ACIGGGVIGG GWVARFLLAG IDVKVFDPHP EAERIVAEVL ANAERAYGLL
     TSVPLPPRGR LTFCASVGEA VADAEWIQES VPERLDLKRR VLAEIDAAAP ADALIGSSTS
     GLLPSDLQEG LGHPERLFVA HPYNPVYLLP LAEIVGGKAT SAATIARAKD ALDAIGMKGV
     VIAREIEAFV GDRLLEALWR EALWLIKDDI CDVETLDDVI RYSFGLRWAQ MGLFQTYRIA
     GGEAGMRHFL AQFGPCLQWP WTKLTDVVDL DEALVEKIGA QSDAQAKGLS IRQLERIRDE
     NLVGILQALK AGQGGEGWGA GKLLAEFEQR LRESAGHADA VDIHAPLPLV ETRVSPAWID
     YNGHMTEHRY LQVFGDTTDA LLRLIGADLA YVEGGHSYYT VETHLRHLDE AHLGEALRAT
     CQILSVDEKR IHIFHRLFAG AGNREVATAE QMLLHVDTRA GRATPAPEII LARLRPIATA
     HAQLDAPEGA GRAVGQKRSM AAV
//

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