CNTB_ECOLI
ID CNTB_ECOLI Reviewed; 321 AA.
AC P76254; O07970; O07972;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Carnitine monooxygenase reductase subunit {ECO:0000255|HAMAP-Rule:MF_02098, ECO:0000305};
DE EC=1.14.13.239 {ECO:0000255|HAMAP-Rule:MF_02098, ECO:0000269|PubMed:25440057};
DE AltName: Full=Carnitine monooxygenase beta subunit {ECO:0000255|HAMAP-Rule:MF_02098, ECO:0000305};
GN Name=yeaX; OrderedLocusNames=b1803, JW1792;
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_02098,
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_02098,
CC ECO:0000269|PubMed:25440057};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02098};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02098};
CC Note=Binds 1 2Fe-2S cluster. {ECO:0000255|HAMAP-Rule:MF_02098};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_02098, ECO:0000269|PubMed:25440057}.
CC -!- SUBUNIT: Composed of an oxygenase subunit (yeaW) and a reductase
CC subunit (yeaX). {ECO:0000250|UniProtKB:D0C9N8}.
CC -!- SIMILARITY: Belongs to the PDR/VanB family. CntB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02098, ECO:0000305}.
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DR EMBL; U00096; AAC74873.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15598.1; -; Genomic_DNA.
DR PIR; C64941; C64941.
DR RefSeq; NP_416317.1; NC_000913.3.
DR RefSeq; WP_001287026.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P76254; -.
DR SMR; P76254; -.
DR BioGRID; 4260337; 16.
DR STRING; 511145.b1803; -.
DR BindingDB; P76254; -.
DR PaxDb; P76254; -.
DR PRIDE; P76254; -.
DR EnsemblBacteria; AAC74873; AAC74873; b1803.
DR EnsemblBacteria; BAA15598; BAA15598; BAA15598.
DR GeneID; 946329; -.
DR KEGG; ecj:JW1792; -.
DR KEGG; eco:b1803; -.
DR PATRIC; fig|1411691.4.peg.450; -.
DR EchoBASE; EB3283; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_17_0_6; -.
DR InParanoid; P76254; -.
DR OMA; CGTCETD; -.
DR PhylomeDB; P76254; -.
DR BioCyc; EcoCyc:G6989-MON; -.
DR BioCyc; MetaCyc:G6989-MON; -.
DR UniPathway; UPA00117; -.
DR PRO; PR:P76254; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
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 1: Evidence at protein level;
KW 2Fe-2S; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; NAD; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..321
FT /note="Carnitine monooxygenase reductase subunit"
FT /id="PRO_0000189405"
FT DOMAIN 4..109
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098"
FT DOMAIN 233..321
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 270
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098"
FT BINDING 275
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098"
FT BINDING 278
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098"
FT BINDING 308
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098"
SQ SEQUENCE 321 AA; 35661 MW; BD34122B24C08DBC CRC64;
MSDYQMFEVQ VSQVEPLTEQ VKRFTLVATD GKPLPAFTGG SHVIVQMSDG DNQYSNAYSL
LSSPHDTSCY QIAVRLEENS RGGSRFLHQQ VKVGDRLTIS TPNNLFALIP SARKHLFIAG
GIGITPFLSH MAELQHSDVD WQLHYCSRNP ESCAFRDELV QHPQAEKVHL HHSSTGTRLE
LARLLADIEP GTHVYTCGPE ALIEAVRSEA ARLDIAADTL HFEQFAIEDK TGDAFTLVLA
RSGKEFVVPE EMTILQVIEN NKAAKVECLC REGVCGTCET AILEGEADHR DQYFSDEERA
SQQSMLICCS RAKGKRLVLD L
