ID   BODG_RHILO              Reviewed;         383 AA.
AC   Q98KK0;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Probable gamma-butyrobetaine dioxygenase;
DE            EC=1.14.11.1;
DE   AltName: Full=Gamma-butyrobetaine hydroxylase;
DE            Short=Gamma-BBH;
DE   AltName: Full=Gamma-butyrobetaine,2-oxoglutarate dioxygenase;
GN   OrderedLocusNames=mll1440;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- FUNCTION: Catalyzes the formation of L-carnitine from gamma-
CC       butyrobetaine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine
CC         + CO2 + succinate; Xref=Rhea:RHEA:24028, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16244, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:17126, ChEBI:CHEBI:30031; EC=1.14.11.1;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family. {ECO:0000305}.
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DR   EMBL; BA000012; BAB48814.1; -; Genomic_DNA.
DR   RefSeq; WP_010910167.1; NC_002678.2.
DR   AlphaFoldDB; Q98KK0; -.
DR   SMR; Q98KK0; -.
DR   STRING; 266835.14022204; -.
DR   PRIDE; Q98KK0; -.
DR   EnsemblBacteria; BAB48814; BAB48814; BAB48814.
DR   KEGG; mlo:mll1440; -.
DR   PATRIC; fig|266835.9.peg.1162; -.
DR   eggNOG; COG2175; Bacteria.
DR   HOGENOM; CLU_021859_2_2_5; -.
DR   OMA; EEKVCIQ; -.
DR   OrthoDB; 819440at2; -.
DR   UniPathway; UPA00118; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008336; F:gamma-butyrobetaine dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0045329; P:carnitine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.2020.30; -; 1.
DR   Gene3D; 3.60.130.10; -; 1.
DR   InterPro; IPR012775; GBBH.
DR   InterPro; IPR010376; GBBH-like_N.
DR   InterPro; IPR038492; GBBH-like_N_sf.
DR   InterPro; IPR042098; TauD-like_sf.
DR   InterPro; IPR003819; TauD/TfdA-like.
DR   Pfam; PF06155; GBBH-like_N; 1.
DR   Pfam; PF02668; TauD; 1.
DR   TIGRFAMs; TIGR02409; carnitine_bodg; 1.
PE   3: Inferred from homology;
KW   Carnitine biosynthesis; Cytoplasm; Dioxygenase; Iron; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN           1..383
FT                   /note="Probable gamma-butyrobetaine dioxygenase"
FT                   /id="PRO_0000207090"
FT   BINDING         201
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   383 AA;  42394 MW;  866A57727B377860 CRC64;
     MLTHALIGDE GRTIELGWQG GRRTRFHAMW LRDNALDDKT RSAGNGQRLI TILDIPAETR
     IGAAEIKGGA LEVSFVPEGK TVSFPAQWLS ANAYDRDELR EPGWTGDVIQ RWTKATMQNS
     VPRASYKAAF HGRSVLREWL SAVRTYGFAV MDGLPAESGA LCKVSDLFGY IRETNYGRWF
     EVRAEVNPNN LAYTNLGLQA HTDNPYRDPV PTLQILACVE NTVEGGESSV IDGFAVAAAL
     QAENPEGFRL LSSCPARFEY AGSSGVRLQA KRPMIELGPD GELICIRFNN RSLAPVVDVP
     FADMDAYYAA YRRFAELIED PDFEVTFKLQ PGQAFIVDNT RVMHARKAFS GTGKRWLQGC
     YADKDGLLST LAAIEHSFKE AAE