ID   PDUW_KLEP7              Reviewed;         404 AA.
AC   A6TDE9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Propionate kinase {ECO:0000255|HAMAP-Rule:MF_01882};
DE            EC=2.7.2.15 {ECO:0000255|HAMAP-Rule:MF_01882};
GN   Name=pduW {ECO:0000255|HAMAP-Rule:MF_01882};
GN   OrderedLocusNames=KPN78578_31590; ORFNames=KPN_03222;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Works with phosphate acetyltransferase (pta) to capture
CC       exogenous propionate and regenerate propionyl-CoA during degradation of
CC       1,2-propanediol (1,2-PD). {ECO:0000250|UniProtKB:P74879}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + propanoate = ADP + propanoyl phosphate;
CC         Xref=Rhea:RHEA:23148, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58933, ChEBI:CHEBI:456216; EC=2.7.2.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01882};
CC   -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC       {ECO:0000250|UniProtKB:P74879, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01882}.
CC   -!- SIMILARITY: Belongs to the acetokinase family. PduW subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01882}.
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DR   EMBL; CP000647; ABR78620.1; -; Genomic_DNA.
DR   RefSeq; WP_015958924.1; NC_009648.1.
DR   AlphaFoldDB; A6TDE9; -.
DR   SMR; A6TDE9; -.
DR   STRING; 272620.KPN_03222; -.
DR   EnsemblBacteria; ABR78620; ABR78620; KPN_03222.
DR   KEGG; kpn:KPN_03222; -.
DR   HOGENOM; CLU_020352_0_1_6; -.
DR   OMA; PLPWRYY; -.
DR   UniPathway; UPA00621; -.
DR   Proteomes; UP000000265; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008980; F:propionate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019543; P:propionate catabolic process; IEA:InterPro.
DR   HAMAP; MF_00020; Acetate_kinase; 1.
DR   HAMAP; MF_01882; Propion_kin_subfam2; 1.
DR   InterPro; IPR004372; Ac/propionate_kinase.
DR   InterPro; IPR000890; Aliphatic_acid_kin_short-chain.
DR   InterPro; IPR023865; Aliphatic_acid_kinase_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR024896; Propionate_kinase_PduW.
DR   PANTHER; PTHR21060; PTHR21060; 1.
DR   Pfam; PF00871; Acetate_kinase; 1.
DR   PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR   PRINTS; PR00471; ACETATEKNASE.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR00016; ackA; 1.
DR   PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR   PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..404
FT                   /note="Propionate kinase"
FT                   /id="PRO_0000398200"
SQ   SEQUENCE   404 AA;  43619 MW;  3E5DCD2D18C89AC4 CRC64;
     MTYKIMAINA GSSSLKFQLL NMPQGALLCQ GLIERIGLPE ARFTLKTSAQ KWQETLPIAD
     HHEAVTLLLE ALTGRGILSS LQEIDGVGHR VAHGGERFKD AALVCDDTLR EIERLAELAP
     LHNPVNALGI RLFRQLLPAV PAVAVFDTAF HQTLAPEAWL YPLPWRYYAE LGIRRYGFHG
     TSHHYVSSAL AEKLGVPLSA LRVVSCHLGN GCSVCAIKGG QSVNTSMGFT PQSGVMMGTR
     SGDLDPSILP WLVEKEGKSA QQLSQLLNNE SGLLGVSGVS SDYRDVEQAA DAGNERAALA
     LSLFAERIRA TIGSYIMQMG GLDALIFTGG IGENSARARA AICRNLHFLG LALDDEKNQR
     SATFIQADNA LVKVAVINTN EELMIARDVM RLALPQAREL AVSA