ID   BODG_PSESK              Reviewed;         383 AA.
AC   P80193;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=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;
OS   Pseudomonas sp. (strain AK-1).
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=29440;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8504802; DOI=10.1111/j.1432-1033.1993.tb17855.x;
RA   Rueetschi U., Nordin I., Odelhoeg B., Joernvall H., Lindstedt S.;
RT   "Gamma-butyrobetaine hydroxylase. Structural characterization of the
RT   Pseudomonas enzyme.";
RL   Eur. J. Biochem. 213:1075-1080(1993).
CC   -!- FUNCTION: Catalyzes the formation of L-carnitine from gamma-
CC       butyrobetaine.
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;
CC   -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family. {ECO:0000305}.
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   AlphaFoldDB; P80193; -.
DR   SMR; P80193; -.
DR   ChEMBL; CHEMBL3817724; -.
DR   PRIDE; P80193; -.
DR   BioCyc; MetaCyc:MON-8461; -.
DR   BRENDA; 1.14.11.1; 5085.
DR   UniPathway; UPA00118; -.
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   1: Evidence at protein level;
KW   Carnitine biosynthesis; Cytoplasm; Dioxygenase; Direct protein sequencing;
KW   Iron; Metal-binding; Oxidoreductase; Zinc.
FT   CHAIN           1..383
FT                   /note="Gamma-butyrobetaine dioxygenase"
FT                   /id="PRO_0000207089"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   VARIANT         1
FT                   /note="Missing (in 50% of the chains)"
SQ   SEQUENCE   383 AA;  43322 MW;  1A16205902C92DB9 CRC64;
     NAIADYRTFP LISPLASAAS FASGVSVTWA DGRVSPFHNL WLRDNCPCGD CVYEVTREQV
     FLVADVPEDI QVQAVTIGDD GRLVVQWDDG HASAYHPGWL RAHAYDAQSL AEREAARPHK
     HRWMQGLSLP VYDHGAVMQD DDTLLEWLLA VRDVGLTQLH GVPTEPGALI PLAKRISFIR
     ESNFGVLFDV RSKADADSNA YTAFNLPLHT DLPTRELQPG LQFLHCLVND ATGGNSTFVD
     GFAIAEALRI EAPAAYRLLC ETPVEFRNKD RHSDYRCTAP VIALDSSGEV REIRLANFLR
     APFQMDAQRM PDYYLAYRRF IQMTREPRFC FTRRLEAGQL WCFDNRRVLH ARDAFDPASG
     DRHFQGCYVD RDELLSRILV LQR