CNTB_ACIB2
ID CNTB_ACIB2 Reviewed; 318 AA.
AC D0C9N8;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 82.
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:24591617};
DE AltName: Full=Carnitine monooxygenase beta subunit {ECO:0000255|HAMAP-Rule:MF_02098, ECO:0000305};
GN Name=cntB {ECO:0000303|PubMed:24591617};
GN ORFNames=F911_03117 {ECO:0000312|EMBL:ENW73703.1},
GN HMPREF0010_01351 {ECO:0000312|EMBL:EEX03957.1};
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, AND DISRUPTION PHENOTYPE.
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_02098, 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_02098,
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_02098,
CC ECO:0000269|PubMed:24591617};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P33164,
CC 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 ECO:0000255|PROSITE-ProRule:PRU00465};
CC Note=Binds 1 2Fe-2S cluster. {ECO:0000255|HAMAP-Rule:MF_02098,
CC ECO:0000255|PROSITE-ProRule:PRU00465};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_02098, 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 PDR/VanB family. CntB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02098, ECO:0000305}.
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DR EMBL; GG704573; EEX03957.1; -; Genomic_DNA.
DR EMBL; APRG01000016; ENW73703.1; -; Genomic_DNA.
DR RefSeq; WP_000146428.1; NZ_KB849991.1.
DR AlphaFoldDB; D0C9N8; -.
DR SMR; D0C9N8; -.
DR EnsemblBacteria; EEX03957; EEX03957; HMPREF0010_01351.
DR GeneID; 66398202; -.
DR PATRIC; fig|575584.18.peg.3257; -.
DR BioCyc; MetaCyc:MON-18570; -.
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: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.
FT CHAIN 1..318
FT /note="Carnitine monooxygenase reductase subunit"
FT /id="PRO_0000442688"
FT DOMAIN 5..107
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098,
FT ECO:0000255|PROSITE-ProRule:PRU00716"
FT DOMAIN 233..318
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 267
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098,
FT ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 272
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098,
FT ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 275
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098,
FT ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 305
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02098,
FT ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 318 AA; 35538 MW; 9D5C7FE49B27D0EF CRC64;
MASHYEMFPA VVTRVEQLTP LIKRFTFKRQ DGQNFPRFSG GSHIIVKMNE QLSNAYSLMS
CTQDLSTYQV CVRKDVEGKG GSVFMHDQCN EGCEIQISEP KNLFPLAETG NKHILIAGGI
GITPFLPQMD ELAARGAEYE LHYAYRSPEH AALLDELTQK HAGHVFSYVD SEGSMLNLDE
LISSQPKGTH VYVCGPKPMI DAVIDCCNKH RYRDEYIHWE QFASTVPEDG EAFTVVLAKS
NQEIEVQSNQ TILQAIETLN IDVECLCREG VCGTCETAIL EGEAEHFDQY LSDAEKASQK
SMMICVSRAK GKKLVLDL
