CNTA_ACIB2
ID CNTA_ACIB2 Reviewed; 371 AA.
AC D0C9N6;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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:24591617};
DE AltName: Full=Carnitine monooxygenase alpha subunit {ECO:0000255|HAMAP-Rule:MF_02097, ECO:0000305};
GN Name=cntA {ECO:0000303|PubMed:24591617};
GN ORFNames=F911_03119 {ECO:0000312|EMBL:ENW73705.1},
GN HMPREF0010_01349 {ECO:0000312|EMBL:EEX03955.1};
OS Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / JCM 6841 / CCUG
OS 19606 / CIP 70.34 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=575584;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC
RC 109757 / NCIMB 12457 / NCTC 12156 / 81;
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC
RC 109757 / NCIMB 12457 / NCTC 12156 / 81;
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Acinetobacter baumannii CIP 70.34T.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLU-205.
RC STRAIN=ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC
RC 109757 / NCIMB 12457 / NCTC 12156 / 81;
RX PubMed=24591617; DOI=10.1073/pnas.1316569111;
RA Zhu Y., Jameson E., Crosatti M., Schaefer H., Rajakumar K., Bugg T.D.,
RA Chen Y.;
RT "Carnitine metabolism to trimethylamine by an unusual Rieske-type oxygenase
RT from human microbiota.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4268-4273(2014).
CC -!- FUNCTION: Converts carnitine to trimethylamine and malic semialdehyde.
CC {ECO:0000255|HAMAP-Rule:MF_02097, ECO:0000269|PubMed:24591617}.
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:24591617};
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:24591617};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02097,
CC ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_02097, ECO:0000255|PROSITE-ProRule:PRU00628};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q53122,
CC ECO:0000255|HAMAP-Rule:MF_02097};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:Q53122,
CC ECO:0000255|HAMAP-Rule:MF_02097};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_02097, ECO:0000269|PubMed:24591617}.
CC -!- SUBUNIT: Composed of an oxygenase subunit (cntA) and a reductase
CC subunit (cntB). {ECO:0000269|PubMed:24591617}.
CC -!- DISRUPTION PHENOTYPE: Mutant cannot grow on carnitine as a sole carbon
CC and energy source, whereas the growth on succinate is not affected.
CC Mutation abolishes trimethylamine formation from carnitine.
CC {ECO:0000269|PubMed:24591617}.
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; GG704573; EEX03955.1; -; Genomic_DNA.
DR EMBL; APRG01000016; ENW73705.1; -; Genomic_DNA.
DR RefSeq; WP_001277086.1; NZ_MJHA01000009.1.
DR PDB; 6Y9C; X-ray; 1.80 A; A=1-371.
DR PDBsum; 6Y9C; -.
DR AlphaFoldDB; D0C9N6; -.
DR SMR; D0C9N6; -.
DR EnsemblBacteria; EEX03955; EEX03955; HMPREF0010_01349.
DR PATRIC; fig|575584.18.peg.3259; -.
DR BioCyc; MetaCyc:MON-18569; -.
DR BRENDA; 1.14.13.239; 98.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000005740; Unassembled WGS sequence.
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; 3D-structure; Iron; Iron-sulfur; Metal-binding; NAD; NADP;
KW Oxidoreductase.
FT CHAIN 1..371
FT /note="Carnitine monooxygenase oxygenase subunit"
FT /id="PRO_0000442686"
FT DOMAIN 44..152
FT /note="Rieske"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 86
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 88
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 106
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 109
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02097,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 208
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q53122, ECO:0000255|HAMAP-
FT Rule:MF_02097"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q53122, ECO:0000255|HAMAP-
FT Rule:MF_02097"
FT BINDING 323
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q53122, ECO:0000255|HAMAP-
FT Rule:MF_02097"
FT MUTAGEN 205
FT /note="E->A,D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24591617"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:6Y9C"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:6Y9C"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:6Y9C"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 183..194
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 220..229
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 231..240
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:6Y9C"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 275..287
FT /evidence="ECO:0007829|PDB:6Y9C"
FT STRAND 290..300
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 306..317
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 319..333
FT /evidence="ECO:0007829|PDB:6Y9C"
FT HELIX 357..367
FT /evidence="ECO:0007829|PDB:6Y9C"
SQ SEQUENCE 371 AA; 42603 MW; 104009D5067F165F CRC64;
MSAVEKLPED FCANPDVAWT FPKVFYTSSQ VFEHEKEAIF AKSWICVAHS SELAQPNDYI
TRKVIGENIV IIRGKDSVLR AFYNVCPHRG HELLSGSGKA KNVITCPYHA WTFKLDGSLA
LARNCDHVES FDKENSSMVP LKVEEYAGFL FINMDENATC VEDQLPGFAE RLNQACGVIK
DLKLAARFVT ETPANWKVIV DNYMECYHCG PAHPGFADSV QVDKYWHTTH QNWTLQYGFA
RSSEKSFKLD PSVTDPEFHG FWTWPCTMFN VPPGSNFMTV IYEFPVDAET TLQHYDIYFT
NEELTQDQKD LIEWYRNVFR PEDLNLVESV QRGLKSRGYR GQGRIMTDKQ RSGISEHGIA
YFQHLVAQYH Q
