ID   PDUX_CITFR              Reviewed;         288 AA.
AC   B1VB82;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=L-threonine kinase;
DE            EC=2.7.1.177 {ECO:0000250|UniProtKB:Q9XDM4};
GN   Name=pduX {ECO:0000303|PubMed:18332146};
OS   Citrobacter freundii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX   NCBI_TaxID=546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX   PubMed=18332146; DOI=10.1074/jbc.m709214200;
RA   Parsons J.B., Dinesh S.D., Deery E., Leech H.K., Brindley A.A., Heldt D.,
RA   Frank S., Smales C.M., Lunsdorf H., Rambach A., Gass M.H., Bleloch A.,
RA   McClean K.J., Munro A.W., Rigby S.E.J., Warren M.J., Prentice M.B.;
RT   "Biochemical and Structural Insights into Bacterial Organelle Form and
RT   Biogenesis.";
RL   J. Biol. Chem. 283:14366-14375(2008).
CC   -!- FUNCTION: L-threonine kinase that catalyzes the conversion of L-
CC       threonine to L-threonine-O-3-phosphate. Involved in the de novo
CC       synthesis of adenosylcobalamin (coenzyme B12) and the assimilation of
CC       cobyric acid. {ECO:0000250|UniProtKB:Q9XDM4}.
CC   -!- FUNCTION: Expression of a cosmid containing the full 21-gene pdu operon
CC       in E.coli allows E.coli to grow on 1,2-propanediol (1,2-PD) with the
CC       appearance of bacterial microcompartments (BMC) in its cytoplasm.
CC       {ECO:0000269|PubMed:18332146}.
CC   -!- FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC)
CC       concentrates low levels of 1,2-PD catabolic enzymes, concentrates
CC       volatile reaction intermediates thus enhancing pathway flux and keeps
CC       the level of toxic, mutagenic propionaldehyde low (Probable). This gene
CC       probably benefits from its induction via the Pdu promoter, rather than
CC       a physical interaction with the BMC (By similarity).
CC       {ECO:0000250|UniProtKB:Q9XDM4, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonine = ADP + H(+) + O-phospho-L-threonine;
CC         Xref=Rhea:RHEA:33707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57926, ChEBI:CHEBI:58675, ChEBI:CHEBI:456216;
CC         EC=2.7.1.177; Evidence={ECO:0000250|UniProtKB:Q9XDM4};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000305}.
CC   -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC       {ECO:0000269|PubMed:18332146}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. PduX subfamily.
CC       {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   EMBL; AM498294; CAM57303.1; -; Genomic_DNA.
DR   RefSeq; WP_046275680.1; NZ_LIDR01000043.1.
DR   GeneID; 66273903; -.
DR   UniPathway; UPA00148; -.
DR   UniPathway; UPA00621; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR012363; PduX.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR43527:SF1; PTHR43527:SF1; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF033887; PduX; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cobalamin biosynthesis; Cytoplasm; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..288
FT                   /note="L-threonine kinase"
FT                   /id="PRO_0000454286"
FT   BINDING         80..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   288 AA;  31681 MW;  5484D4E86AD85EEE CRC64;
     MAVAQCPASC GELIQGWILG SEKLVSCPVE WYSTVEVTSG SPLTDERPLS RAMVDRLLQH
     WQYPAHLSQD IRIDVQSTIP IAKGMASSTA DIAATAIAAA HYLGHQLDEP TLAQLCVSLE
     PTDSTVFRKL TLFDHNNAST QIGCEAQPQL DLLVLESPET LRTADYHRIP RHSGLQAGAA
     ALQRAWEKVQ EACISQNPYR LGEAATLSAI ASQLLLPKPD FDSLLALVEE CDLYGVNVAH
     SGSVVGLMLD RNRHDVDYIK WMLTQKKLTI HWPEQHLLRM VTGGVELQ