(data stored in ACNUC1104 zone)

SWISSPROT: D3VIU1_XENNA

ID   D3VIU1_XENNA            Unreviewed;       321 AA.
AC   D3VIU1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Carnitine monooxygenase reductase subunit {ECO:0000256|HAMAP-Rule:MF_02098};
DE            EC=1.14.13.239 {ECO:0000256|HAMAP-Rule:MF_02098};
DE   AltName: Full=Carnitine monooxygenase beta subunit {ECO:0000256|HAMAP-Rule:MF_02098};
GN   Name=yeaX {ECO:0000313|EMBL:CBJ88641.1};
GN   OrderedLocusNames=XNC1_0567 {ECO:0000313|EMBL:CBJ88641.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88641.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88641.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Converts carnitine to trimethylamine and malic
CC       semialdehyde. {ECO:0000256|HAMAP-Rule:MF_02098}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + H(+) + NADH + O2 = (3R)-3-hydroxy-4-
CC         oxobutanoate + H2O + NAD(+) + trimethylamine;
CC         Xref=Rhea:RHEA:55396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16347, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58389, ChEBI:CHEBI:138809;
CC         EC=1.14.13.239; Evidence={ECO:0000256|HAMAP-Rule:MF_02098};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + H(+) + NADPH + O2 = (3R)-3-hydroxy-4-
CC         oxobutanoate + H2O + NADP(+) + trimethylamine;
CC         Xref=Rhea:RHEA:55368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16347, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:58389, ChEBI:CHEBI:138809;
CC         EC=1.14.13.239; Evidence={ECO:0000256|HAMAP-Rule:MF_02098};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02098};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02098};
CC       Note=Binds 1 2Fe-2S cluster. {ECO:0000256|HAMAP-Rule:MF_02098};
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_02098}.
CC   -!- SUBUNIT: Composed of an oxygenase subunit and a reductase subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_02098}.
CC   -!- SIMILARITY: Belongs to the PDR/VanB family. CntB subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02098}.
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DR   EMBL; FN667742; CBJ88641.1; -; Genomic_DNA.
DR   RefSeq; WP_010848971.1; NC_014228.1.
DR   STRING; 406817.XNC1_0567; -.
DR   EnsemblBacteria; CBJ88641; CBJ88641; XNC1_0567.
DR   KEGG; xne:XNC1_0567; -.
DR   eggNOG; ENOG4105E3J; Bacteria.
DR   eggNOG; COG1018; LUCA.
DR   HOGENOM; HOG000141052; -.
DR   KO; K22444; -.
DR   OMA; QPLGTHV; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:UniProtKB-UniRule.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
DR   HAMAP; MF_02098; Carnitine_monoox_B; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR039003; Carnitine_monoox_B.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR000951; Ph_dOase_redase.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VIU1.
DR   SWISS-2DPAGE; D3VIU1.
KW   2Fe-2S {ECO:0000256|HAMAP-Rule:MF_02098,
KW   ECO:0000256|SAAS:SAAS00660781};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02098,
KW   ECO:0000256|SAAS:SAAS01058804};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_02098};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_02098, ECO:0000256|SAAS:SAAS00909025};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02098,
KW   ECO:0000256|SAAS:SAAS00908250};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02098,
KW   ECO:0000256|SAAS:SAAS00909276};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_02098};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_02098};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02098,
KW   ECO:0000313|EMBL:CBJ88641.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   DOMAIN        4    109       FAD-binding FR-type.
FT                                {ECO:0000259|PROSITE:PS51384}.
FT   DOMAIN      235    321       2Fe-2S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51085}.
FT   METAL       270    270       Iron-sulfur (2Fe-2S). {ECO:0000256|HAMAP-
FT                                Rule:MF_02098}.
FT   METAL       275    275       Iron-sulfur (2Fe-2S). {ECO:0000256|HAMAP-
FT                                Rule:MF_02098}.
FT   METAL       278    278       Iron-sulfur (2Fe-2S). {ECO:0000256|HAMAP-
FT                                Rule:MF_02098}.
FT   METAL       308    308       Iron-sulfur (2Fe-2S). {ECO:0000256|HAMAP-
FT                                Rule:MF_02098}.
SQ   SEQUENCE   321 AA;  35634 MW;  8CE57DB6A05AC361 CRC64;
     MSIYQTISVI VSNIEAITPN IKRFTLIPAE NTQLPAFTGG SHIFVQMQDG DKRYSNAYSL
     LSSPFDKHSY QIAVKREEHS RGGSAFMHDK VVIGNTLIIS EPNNLFALVP GAKKHILIAG
     GIGITPFMSH LYELKHQDAE YELHYCYRNS DDNAFTQELM AAGFKAKIDC YISSEGTRLE
     LDTLISRLPE GSHVYTCGSS ALNNGVKQAA QNAGFPDHQL HFEQFTIEDK TGDAFTVVLA
     KSGIELEVDS ESTILQVIER NKAVHVECMC REGVCGTCET MILEGEADHR DQYLSDEEKQ
     SQTSMLICCS RAKGKRLVLD L
//

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