ID D4B6D9_9ENTR Unreviewed; 374 AA.
AC D4B6D9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=CIT292_06777 {ECO:0000313|EMBL:EFE10598.1};
OS Citrobacter youngae ATCC 29220.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=500640 {ECO:0000313|EMBL:EFE10598.1, ECO:0000313|Proteomes:UP000003880};
RN [1] {ECO:0000313|EMBL:EFE10598.1, ECO:0000313|Proteomes:UP000003880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29220 {ECO:0000313|EMBL:EFE10598.1,
RC ECO:0000313|Proteomes:UP000003880};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) 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:EFE10598.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABWL02000002; EFE10598.1; -; Genomic_DNA.
DR RefSeq; WP_006684197.1; NZ_GG730299.1.
DR AlphaFoldDB; D4B6D9; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_3_0_6; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000003880; 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 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 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 325
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02097"
SQ SEQUENCE 374 AA; 42724 MW; A6FB09BCAE2D87B7 CRC64;
MSNLSPEFIL PQNFCANPQD AWTIPARFYT DQQAFEHEQE HVFAKSWICV AHGSELAKPN
DYVTREVIGE NIVLVRGRDN VLRAFYNVCP HRGHQLLSGE GKAKNVITCP YHAWAFKLDG
NLAHARNCEN VANFDSEKAH LTPVRLEEYA GFVFINMDPN AGSVEEQLPG LADKVIEACP
EVHDLKLAAR FTTRTPANWK NIVDNYLECY HCGPAHPGFS DSVQVDRYWH TMHGNWTLQY
GFAKPSEQSF KFEEGVDAAF HGFWLWPCTM LNVTPIKGMM TVIYEFPVDA ETTLQNYDIY
FTNEELTEEQ KELIEWYRNV FRPEDLRLVE SVQKGLKSRG YRGQGRIMAD TSGSGISEHG
IAHFHNLVAQ VFQE
//
