CNTA_ECOLI
ID CNTA_ECOLI Reviewed; 374 AA.
AC P0ABR7; P76253;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Carnitine monooxygenase oxygenase subunit {ECO:0000255|HAMAP-Rule:MF_02097, ECO:0000305};
DE EC=1.14.13.239 {ECO:0000255|HAMAP-Rule:MF_02097, ECO:0000269|PubMed:25440057};
DE AltName: Full=Carnitine monooxygenase alpha subunit {ECO:0000255|HAMAP-Rule:MF_02097, ECO:0000305};
GN Name=yeaW; OrderedLocusNames=b1802, JW5294;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=K12 / DH10B;
RX PubMed=25440057; DOI=10.1016/j.cmet.2014.10.006;
RA Koeth R.A., Levison B.S., Culley M.K., Buffa J.A., Wang Z., Gregory J.C.,
RA Org E., Wu Y., Li L., Smith J.D., Tang W.H., DiDonato J.A., Lusis A.J.,
RA Hazen S.L.;
RT "Gamma-butyrobetaine is a proatherogenic intermediate in gut microbial
RT metabolism of L-carnitine to TMAO.";
RL Cell Metab. 20:799-812(2014).
CC -!- FUNCTION: Converts carnitine to trimethylamine and malic semialdehyde.
CC Can also use gamma-butyrobetaine, choline and betaine as substrates.
CC {ECO:0000269|PubMed:25440057}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + H(+) + NADH + O2 = (3R)-3-hydroxy-4-
CC oxobutanoate + H2O + NAD(+) + trimethylamine; Xref=Rhea:RHEA:55396,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58389, ChEBI:CHEBI:138809; EC=1.14.13.239;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02097,
CC ECO:0000269|PubMed:25440057};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + H(+) + NADPH + O2 = (3R)-3-hydroxy-4-
CC oxobutanoate + H2O + NADP(+) + trimethylamine; Xref=Rhea:RHEA:55368,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58389, ChEBI:CHEBI:138809; EC=1.14.13.239;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02097,
CC ECO:0000269|PubMed:25440057};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02097};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_02097};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02097};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000255|HAMAP-Rule:MF_02097};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_02097, ECO:0000269|PubMed:25440057}.
CC -!- SUBUNIT: Composed of an oxygenase subunit (yeaW) and a reductase
CC subunit (yeaX). {ECO:0000250|UniProtKB:D0C9N6}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. CntA subfamily. {ECO:0000255|HAMAP-Rule:MF_02097,
CC ECO:0000305}.
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DR EMBL; U00096; AAC74872.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15597.2; -; Genomic_DNA.
DR PIR; B64941; B64941.
DR RefSeq; NP_416316.1; NC_000913.3.
DR RefSeq; WP_000067822.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P0ABR7; -.
DR SMR; P0ABR7; -.
DR BioGRID; 4259149; 7.
DR STRING; 511145.b1802; -.
DR BindingDB; P0ABR7; -.
DR PaxDb; P0ABR7; -.
DR PRIDE; P0ABR7; -.
DR EnsemblBacteria; AAC74872; AAC74872; b1802.
DR EnsemblBacteria; BAA15597; BAA15597; BAA15597.
DR GeneID; 66674309; -.
DR GeneID; 946325; -.
DR KEGG; ecj:JW5294; -.
DR KEGG; eco:b1802; -.
DR PATRIC; fig|1411691.4.peg.451; -.
DR EchoBASE; EB3282; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_3_0_6; -.
DR InParanoid; P0ABR7; -.
DR OMA; NIMVEWY; -.
DR PhylomeDB; P0ABR7; -.
DR BioCyc; EcoCyc:G6988-MON; -.
DR BioCyc; MetaCyc:G6988-MON; -.
DR UniPathway; UPA00117; -.
DR PRO; PR:P0ABR7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
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 PANTHER; PTHR43756; PTHR43756; 1.
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 1: Evidence at protein level;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..374
FT /note="Carnitine monooxygenase oxygenase subunit"
FT /id="PRO_0000085063"
FT DOMAIN 47..155
FT /note="Rieske"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
FT BINDING 89
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
FT BINDING 91
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
FT BINDING 109
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
FT BINDING 112
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
FT BINDING 211
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
FT BINDING 216
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
FT BINDING 325
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
SQ SEQUENCE 374 AA; 42561 MW; BB5386ACA9585606 CRC64;
MSNLSPDFVL PENFCANPQE AWTIPARFYT DQNAFEHEKE NVFAKSWICV AHSSELANAN
DYVTREIIGE SIVLVRGRDK VLRAFYNVCP HRGHQLLSGE GKAKNVITCP YHAWAFKLDG
NLAHARNCEN VANFDSDKAQ LVPVRLEEYA GFVFINMDPN ATSVEDQLPG LGAKVLEACP
EVHDLKLAAR FTTRTPANWK NIVDNYLECY HCGPAHPGFS DSVQVDRYWH TMHGNWTLQY
GFAKPSEQSF KFEEGTDAAF HGFWLWPCTM LNVTPIKGMM TVIYEFPVDS ETTLQNYDIY
FTNEELTDEQ KSLIEWYRDV FRPEDLRLVE SVQKGLKSRG YRGQGRIMAD SSGSGISEHG
IAHFHNLLAQ VFKD
