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Database: UniProt
Entry: A0A1I2FG14_9BACI
LinkDB: A0A1I2FG14_9BACI
Original site: A0A1I2FG14_9BACI 
ID   A0A1I2FG14_9BACI        Unreviewed;       319 AA.
AC   A0A1I2FG14;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   16-JAN-2019, entry version 5.
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   ORFNames=SAMN05428981_11366 {ECO:0000313|EMBL:SFF04454.1};
OS   Bacillus sp. OV194.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1881065 {ECO:0000313|EMBL:SFF04454.1, ECO:0000313|Proteomes:UP000198547};
RN   [1] {ECO:0000313|EMBL:SFF04454.1, ECO:0000313|Proteomes:UP000198547}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV194 {ECO:0000313|EMBL:SFF04454.1,
RC   ECO:0000313|Proteomes:UP000198547};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOML01000013; SFF04454.1; -; Genomic_DNA.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000198547; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000198547};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02129};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_02129};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02129}.
FT   DOMAIN        7    180       3HCDH_N. {ECO:0000259|Pfam:PF02737}.
FT   DOMAIN      186    254       3HCDH. {ECO:0000259|Pfam:PF00725}.
FT   NP_BIND      12     17       NAD. {ECO:0000256|HAMAP-Rule:MF_02129}.
SQ   SEQUENCE   319 AA;  35289 MW;  FDDC460692BD6CE0 CRC64;
     MQSLVKNVTV VGTGVIGNGW ISRFLANGYH VTATDPAPGA EEKMRQAVKS VWSSLEKQGL
     AAGAAPDRLH FEPNLERAVS NADLIQENAP EREELKRSLL KTISHAAKPN AIIASSTSGY
     MPSILQKDCL HPERVIVAHP FNPVYLMPLV ELVGGQQTSS EVMVRAQSFY HSVRMKALIV
     SREIDGHIAD RLMEAIWREA LHLVNDGVAT TEEVDAAIVY GPGLRWALMG PFLTLHMAGG
     KQGMRHMLEQ FGPALKLPWT HLVAPELTEE LAQRVIEGCE KQTDGMDMSI LEKRRDDFLI
     ELTDLLEKYW PSANLNGKL
//
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