(data stored in SCRATCH zone)

SWISSPROT: D3VIT8_XENNA

ID   D3VIT8_XENNA            Unreviewed;       372 AA.
AC   D3VIT8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 53.
DE   RecName: Full=Carnitine monooxygenase oxygenase subunit {ECO:0000256|HAMAP-Rule:MF_02097};
DE            EC=1.14.13.239 {ECO:0000256|HAMAP-Rule:MF_02097};
DE   AltName: Full=Carnitine monooxygenase alpha subunit {ECO:0000256|HAMAP-Rule:MF_02097};
GN   Name=yeaW {ECO:0000313|EMBL:CBJ88638.1};
GN   OrderedLocusNames=XNC1_0564 {ECO:0000313|EMBL:CBJ88638.1};
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:CBJ88638.1, 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:CBJ88638.1, 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_02097}.
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_02097};
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_02097};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02097};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_02097};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02097};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_02097};
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_02097}.
CC   -!- SUBUNIT: Composed of an oxygenase subunit and a reductase subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_02097}.
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
CC       dioxygenase alpha subunit family. CntA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02097}.
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DR   EMBL; FN667742; CBJ88638.1; -; Genomic_DNA.
DR   RefSeq; WP_013183339.1; NC_014228.1.
DR   STRING; 406817.XNC1_0564; -.
DR   EnsemblBacteria; CBJ88638; CBJ88638; XNC1_0564.
DR   KEGG; xne:XNC1_0564; -.
DR   eggNOG; ENOG4105DVW; Bacteria.
DR   eggNOG; COG4638; LUCA.
DR   HOGENOM; HOG000248945; -.
DR   KO; K22443; -.
DR   OMA; TNVVEFY; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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   Gene3D; 2.102.10.10; -; 1.
DR   HAMAP; MF_02097; Carnitine_monoox_A; 1.
DR   InterPro; IPR039004; Carnitine_monoox_A.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR   InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR   InterPro; IPR001663; Rng_hydr_dOase-A.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF00848; Ring_hydroxyl_A; 1.
DR   PRINTS; PR00090; RNGDIOXGNASE.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
DR   PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VIT8.
DR   SWISS-2DPAGE; D3VIT8.
KW   2Fe-2S {ECO:0000256|HAMAP-Rule:MF_02097};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_02097};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02097};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02097};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_02097};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_02097};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02097,
KW   ECO:0000313|EMBL:CBJ88638.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   DOMAIN       47    155       Rieske. {ECO:0000259|PROSITE:PS51296}.
FT   METAL        89     89       Iron-sulfur (2Fe-2S). {ECO:0000256|HAMAP-
FT                                Rule:MF_02097}.
FT   METAL        91     91       Iron-sulfur (2Fe-2S); via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02097}.
FT   METAL       109    109       Iron-sulfur (2Fe-2S). {ECO:0000256|HAMAP-
FT                                Rule:MF_02097}.
FT   METAL       112    112       Iron-sulfur (2Fe-2S); via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02097}.
FT   METAL       211    211       Iron; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02097}.
FT   METAL       216    216       Iron; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02097}.
FT   METAL       323    323       Iron. {ECO:0000256|HAMAP-Rule:MF_02097}.
SQ   SEQUENCE   372 AA;  42468 MW;  10082078D6D1255B CRC64;
     MSIQDPYLTL PRNFCANPAE AYTMPARFYT SQDVFDYEKE AIFAKSWICV AHGSELANPN
     DYVTREIIGE SIVIVRGRDN ILRAFFNVCP HRGHQLLKGE GKAKNVITCP YHAWTFKLDG
     SLAHARNCEN VANFDKGLAQ LTPVKLEEYA GFVFINMDMN AGTVEAQLPG LSTRVLAACP
     DVYDLKLAAR FTTATPANWK SIVDNYLECY HCGPAHPGFS TSVQVDRYWH TMYEKWSLQF
     GYAIPSDQSF KFEGESSFHG FWLWPCTMYN VTPVKGMMTV IYEFPVDAET TLQYYDIYFT
     NEDITEEQKS LIEWYRDVFR PEDLRLVESV QKGLKSRGYR GQGRIMADST GSGISEHGIA
     YFHHLIAQTY HE
//

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