CNTB_ACICP
ID CNTB_ACICP Reviewed; 304 AA.
AC F0KFI7;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
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:8000862};
DE AltName: Full=Carnitine monooxygenase beta subunit {ECO:0000255|HAMAP-Rule:MF_02098, ECO:0000305};
GN Name=yeaX {ECO:0000312|EMBL:ADY80707.1};
GN OrderedLocusNames=BDGL_000121 {ECO:0000312|EMBL:ADY80707.1};
OS Acinetobacter calcoaceticus (strain PHEA-2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=871585;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHEA-2;
RX PubMed=21441526; DOI=10.1128/jb.00261-11;
RA Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z.,
RA Yuan M., Zhou Z., Elmerich C., Lin M.;
RT "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from
RT industry wastewater.";
RL J. Bacteriol. 193:2672-2673(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PATHWAY.
RC STRAIN=ATCC 39648;
RX PubMed=8000862; DOI=10.1016/0968-0896(94)80009-x;
RA Ditullio D., Anderson D., Chen C.S., Sih C.J.;
RT "L-carnitine via enzyme-catalyzed oxidative kinetic resolution.";
RL Bioorg. Med. Chem. 2:415-420(1994).
CC -!- FUNCTION: Converts carnitine to trimethylamine and malic semialdehyde.
CC Acts on both enantiomers. {ECO:0000269|PubMed:8000862}.
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:8000862};
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:8000862};
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 -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:8000862}.
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_02098, ECO:0000269|PubMed:8000862}.
CC -!- SUBUNIT: Composed of an oxygenase subunit and a reductase subunit.
CC {ECO:0000255|HAMAP-Rule:MF_02098}.
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; CP002177; ADY80707.1; -; Genomic_DNA.
DR RefSeq; WP_014205962.1; NC_016603.1.
DR RefSeq; YP_004994389.1; NC_016603.1.
DR AlphaFoldDB; F0KFI7; -.
DR SMR; F0KFI7; -.
DR STRING; 871585.BDGL_000121; -.
DR EnsemblBacteria; ADY80707; ADY80707; BDGL_000121.
DR GeneID; 11638296; -.
DR KEGG; acc:BDGL_000121; -.
DR PATRIC; fig|871585.3.peg.120; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_17_0_6; -.
DR OMA; CETMILE; -.
DR BioCyc; MetaCyc:MON-8605; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000007477; 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; 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; 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..304
FT /note="Carnitine monooxygenase reductase subunit"
FT /id="PRO_0000442689"
FT DOMAIN 1..93
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098"
FT DOMAIN 219..304
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 253
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098"
FT BINDING 258
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098"
FT BINDING 261
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098"
FT BINDING 291
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098"
SQ SEQUENCE 304 AA; 33990 MW; A5B44FC2FC44F015 CRC64;
MEQLTPLIKR FTFKRQDGQN FPRFSGGSHI IVKMNEQISN AYSLMSCTQD LSTYQVCVRK
DVEGKGGSVF MHDQCNEGCE IQISEPKNLF PLAETGNKHI LIAGGIGITP FLPQMDELAA
RGADFELHYA YRSPEHAALL DELKQKHAKH VFSYVDSEGC SLKLDELISS QPKGTHVYVC
GPKPMIDAVI DCCNKHRYRD EYIHWEQFAS TVPEDGEAFT VVLAKSNQEI EVQSNQTILQ
AIETLNIDVE CLCREGVCGT CETAILEGEA DHFDQYLSDA EKASQKSMMI CVSRAKGKKL
VLDL
