ID A0A1C6LXW4_9NEIS Unreviewed; 379 AA.
AC A0A1C6LXW4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=PSELUDRAFT_0960 {ECO:0000313|EMBL:SCK11427.1};
OS Vogesella sp. LIG4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Vogesella.
OX NCBI_TaxID=1192162 {ECO:0000313|EMBL:SCK11427.1, ECO:0000313|Proteomes:UP000198213};
RN [1] {ECO:0000313|EMBL:SCK11427.1, ECO:0000313|Proteomes:UP000198213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LIG4 {ECO:0000313|Proteomes:UP000198213};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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DR EMBL; LT607802; SCK11427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6LXW4; -.
DR OrthoDB; 9790995at2; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000198213; Chromosome i.
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 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 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}; Monooxygenase {ECO:0000313|EMBL:SCK11427.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000198213}.
FT DOMAIN 47..154
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT BINDING 88
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
FT BINDING 90
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
FT BINDING 108
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
FT BINDING 111
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
FT BINDING 210
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
FT BINDING 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
FT BINDING 325
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
SQ SEQUENCE 379 AA; 42615 MW; 3125A387483FBBFD CRC64;
MHSAIGTDLP ADFCQDMDNA YTLPASYYTS EAVFQHEKEH IFTRAWLCLC HASELAESNA
YVTRKIVGEN LVAVRGRDGV LRAFYNVCPH RGHELFKDSG VARNVVSCPY HAWTFKLDGE
LAVARNCEHV ANFDKADYNL VPIRVAEYAG FVFVNMDMDA PPVETALAGL DAHLKTVCPN
VAELQVASRT ITDTPANWKV IVDNYMECYH CAPAHPGFSS SVDSERYTHT FHGNWTLQHG
YSKSSEQGYS FDAEVNNQAF SGYWVWPCVM FNVVPGDDTM TVIYEYPVSA GLTVQYYEVL
MKSKEVSPEQ RNFITWATQT FRPEDLALVE SVQRGLQSRG YRGQGRIMVD ATRSGISEHG
IAYFHNKVAG YYPRSGEEQ
//
