ID E6BER4_ECOLX Unreviewed; 321 AA.
AC E6BER4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 ORFNames=HMPREF9350_00661 {ECO:0000313|EMBL:EFU37354.1};
OS Escherichia coli MS 85-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679202 {ECO:0000313|EMBL:EFU37354.1, ECO:0000313|Proteomes:UP000005056};
RN [1] {ECO:0000313|EMBL:EFU37354.1, ECO:0000313|Proteomes:UP000005056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 85-1 {ECO:0000313|EMBL:EFU37354.1,
RC ECO:0000313|Proteomes:UP000005056};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts carnitine to trimethylamine and malic semialdehyde.
CC {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; 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:0000256|HAMAP-Rule:MF_02098};
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:0000256|HAMAP-Rule:MF_02098};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02098};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFU37354.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADWQ01000002; EFU37354.1; -; Genomic_DNA.
DR RefSeq; WP_001286998.1; NZ_ADWQ01000002.1.
DR AlphaFoldDB; E6BER4; -.
DR PATRIC; fig|679202.3.peg.615; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000005056; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
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 CDD; cd06185; PDR_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
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; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 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;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|HAMAP-Rule:MF_02098};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02098};
KW FMN {ECO:0000256|HAMAP-Rule:MF_02098};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_02098};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_02098}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_02098};
KW NAD {ECO:0000256|HAMAP-Rule:MF_02098};
KW NADP {ECO:0000256|HAMAP-Rule:MF_02098};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02098}.
FT DOMAIN 4..109
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 233..321
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT BINDING 270
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02098"
FT BINDING 275
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02098"
FT BINDING 278
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02098"
FT BINDING 308
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02098"
SQ SEQUENCE 321 AA; 35713 MW; 6FC2D74A52762B8C CRC64;
MSDYQMFEVQ VSQVEPLTEQ VKRFTLVATD GKPLPAFTGG SHIIVQMSDG DNHYSNAYSL
LSSPHDTSCY QIAVRLEENS RGGSRFLHQQ VKVGDRLTIS TPNNLFALIP SARKHLFIAG
GIGITPFLSH MAELQHSDVD WQLHYCSRNP ESCAFRDELV QHPQAEKVHL HHSSTGTRLE
LARLLADIEP GTHVYTCGPE ALNEAVRSEA ARLDIVADTL HFEQFAIEDK TGDAFTLVLA
RSGKEFVVPE EMTILQVIEN NKAAKVECLC REGVCGTCET AILEGEADHR DQYFSDEERA
SQQSMLICCS RAKGKRLVLD L
//
