ID A0A0J5FNC4_9GAMM Unreviewed; 372 AA.
AC A0A0J5FNC4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Carnitine monooxygenase oxygenase subunit {ECO:0000256|HAMAP-Rule:MF_02097};
DE EC=1.14.13.239 {ECO:0000256|HAMAP-Rule:MF_02097};
DE AltName: Full=Carnitine monooxygenase alpha subunit {ECO:0000256|HAMAP-Rule:MF_02097};
GN ORFNames=AB204_19585 {ECO:0000313|EMBL:KMJ43452.1};
OS Xenorhabdus khoisanae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=880157 {ECO:0000313|EMBL:KMJ43452.1, ECO:0000313|Proteomes:UP000036277};
RN [1] {ECO:0000313|EMBL:KMJ43452.1, ECO:0000313|Proteomes:UP000036277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCB {ECO:0000313|EMBL:KMJ43452.1,
RC ECO:0000313|Proteomes:UP000036277};
RA Naidoo S., Featherston J., Gray V.M.;
RT "Draft Whole-Genome Sequence of the Entomopathogenic Bacterium Xenorhabdus
RT khoisanae.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts carnitine to trimethylamine and malic semialdehyde.
CC {ECO:0000256|HAMAP-Rule:MF_02097}.
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_02097};
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_02097};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02097};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000256|HAMAP-Rule:MF_02097};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02097};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_02097};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000256|HAMAP-Rule:MF_02097}.
CC -!- SUBUNIT: Composed of an oxygenase subunit and a reductase subunit.
CC {ECO:0000256|HAMAP-Rule:MF_02097}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. CntA subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_02097}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMJ43452.1}.
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DR EMBL; LFCV01000182; KMJ43452.1; -; Genomic_DNA.
DR RefSeq; WP_047965056.1; NZ_LFCV01000182.1.
DR AlphaFoldDB; A0A0J5FNC4; -.
DR STRING; 880157.AB204_19585; -.
DR PATRIC; fig|880157.4.peg.4222; -.
DR OrthoDB; 9769355at2; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000036277; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
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 CDD; cd08886; RHO_alpha_C_2; 1.
DR CDD; cd03469; Rieske_RO_Alpha_N; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 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; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43756:SF5; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|HAMAP-Rule:MF_02097};
KW Dioxygenase {ECO:0000313|EMBL:KMJ43452.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_02097};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_02097};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_02097};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_02097};
KW NADP {ECO:0000256|HAMAP-Rule:MF_02097};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02097}.
FT DOMAIN 47..155
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT BINDING 89
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
FT BINDING 91
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
FT BINDING 109
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
FT BINDING 112
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
FT BINDING 211
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
FT BINDING 216
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
FT BINDING 323
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
SQ SEQUENCE 372 AA; 42617 MW; 31EBD21FB7F384F7 CRC64;
MSIQHQNFTL PKNFCAIPTE AYTMPARFYT SQDVFDYEKE AIFAKSWICV AHSSELANPN
DYVTREIIGE SIVIVRGRDN VLRAFFNVCP HRGHQLLTGE GKAKNVITCP YHAWTFKLDG
TLAHARNCEN VANFDKDLAQ LSPVKLEEYA GFVFINMDMN AGTVEEQLPG LSAKVLEACP
EVYELKLADR FTTVTPANWK SIVDNYLECY HCGPAHPGFS TSVQVDRYWH TMHEKWSLQF
GYAIPSDQSF KFEGESSFHG FWLWPCTMYN VTPIKGMMTV IYEFPIDAET TLQHYDIYFT
NEDLTQEQKS LIEWYRDVFR PEDLRLVESV QKGLKSRGYP GQGRIMADST GSGISEHGIA
YFHNLIAQIY HE
//
