CNTA_ACICP
ID CNTA_ACICP Reviewed; 371 AA.
AC F0KFI5;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
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:8000862};
DE AltName: Full=Carnitine monooxygenase alpha subunit {ECO:0000255|HAMAP-Rule:MF_02097, ECO:0000305};
GN Name=yeaW {ECO:0000312|EMBL:ADY80705.1};
GN OrderedLocusNames=BDGL_000119 {ECO:0000312|EMBL:ADY80705.1};
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_02097,
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_02097,
CC ECO:0000269|PubMed:8000862};
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 -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:8000862}.
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_02097, ECO:0000269|PubMed:8000862}.
CC -!- SUBUNIT: Composed of an oxygenase subunit and a reductase subunit.
CC {ECO:0000255|HAMAP-Rule:MF_02097}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. CntA subfamily. {ECO:0000255|HAMAP-Rule:MF_02097,
CC ECO:0000305}.
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; CP002177; ADY80705.1; -; Genomic_DNA.
DR RefSeq; WP_002120432.1; NC_016603.1.
DR RefSeq; YP_004994387.1; NC_016603.1.
DR AlphaFoldDB; F0KFI5; -.
DR SMR; F0KFI5; -.
DR STRING; 871585.BDGL_000119; -.
DR EnsemblBacteria; ADY80705; ADY80705; BDGL_000119.
DR GeneID; 11638294; -.
DR KEGG; acc:BDGL_000119; -.
DR PATRIC; fig|871585.3.peg.118; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_3_0_6; -.
DR OMA; NIMVEWY; -.
DR BioCyc; MetaCyc:MON-8604; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000007477; 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 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..371
FT /note="Carnitine monooxygenase oxygenase subunit"
FT /id="PRO_0000442687"
FT DOMAIN 44..152
FT /note="Rieske"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
FT BINDING 86
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
FT BINDING 88
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
FT BINDING 106
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 208
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
FT BINDING 323
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097"
SQ SEQUENCE 371 AA; 42617 MW; 351612E5C2747847 CRC64;
MSAVEKLPED FCANPDVAWT FPKVFYTSSQ VFEHEKEAIF AKSWICVAHG SELAQPNDYI
TRKVIGENIV IIRGKDSVLR AFYNVCPHRG HELLSGSGKA KNVITCPYHA WTFKLDGSLA
LARNCDHVES FDKENSSMVP LKVEEYAGFV FINMDENATC VEDQLPEFAE RLNQACSVIK
DLKLAARFVT ETPANWKVIV DNYLECYHCG PAHPGFADSV QVDKYWHTTH QNWTLQYGFA
RSSEKSFKLD PSVTDPEFHG FWTWPCTMFN VPPGSNFMTV IYEFPVDAET TLQHYDIYFT
NEELTQDQKD LIEWYRNVFR PEDLNLVESV QRGLKSRGYR GQGRIMTDKQ RSGISEHGIA
YFQHLVAQHH K
