ID S6ANB9_PSERE Unreviewed; 322 AA.
AC S6ANB9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, 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=PCA10_47180 {ECO:0000313|EMBL:BAN50450.1};
OS Pseudomonas resinovorans NBRC 106553.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN50450.1, ECO:0000313|Proteomes:UP000015503};
RN [1] {ECO:0000313|EMBL:BAN50450.1, ECO:0000313|Proteomes:UP000015503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN50450.1,
RC ECO:0000313|Proteomes:UP000015503};
RX PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA Fujita N., Nojiri H.;
RT "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT resinovorans Strain CA10 (NBRC 106553).";
RL Genome Announc. 1:e00488-13(2013).
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}.
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DR EMBL; AP013068; BAN50450.1; -; Genomic_DNA.
DR RefSeq; WP_016494579.1; NC_021499.1.
DR AlphaFoldDB; S6ANB9; -.
DR STRING; 1245471.PCA10_47180; -.
DR KEGG; pre:PCA10_47180; -.
DR PATRIC; fig|1245471.3.peg.4778; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_17_0_6; -.
DR OrthoDB; 9801223at2; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000015503; Chromosome.
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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000015503}.
FT DOMAIN 5..110
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 233..322
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 322 AA; 35128 MW; DEAFAA53DCC8FACD CRC64;
MNNLQQIIAV RVAAVEQMTP QIKRFTLAAC DGRPLPGFTG GSHVLVQMTQ GERRFTNAYS
LMSSPADTRH YQIGVRREEN SKGGSAFLHE QVAVGSELRI SLPSNLFALA PEAGHHVLVA
GGIGITPFLS QLHDLRRLGA SYELHYAFRA PEHGAFREEL VAGHGPQCRF YIDSEGQRLD
LDALLDGMAP DAHVYVCGPR PLIDALIERA RAKGIEQARV HWEQFAATPA EGGAFTLVLG
RSGRELQVEE GSSILQAIER SNAAQVECLC REGVCGTCET RILEGQAQHF DQYLTDEEKA
AQQSLMICVS RAAAGSRLVL DL
//