ID   PDUW_YERE8              Reviewed;         412 AA.
AC   A1JTT9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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}; OrderedLocusNames=YE2747;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL12781.1; -; Genomic_DNA.
DR   RefSeq; WP_011816704.1; NC_008800.1.
DR   RefSeq; YP_001006938.1; NC_008800.1.
DR   AlphaFoldDB; A1JTT9; -.
DR   SMR; A1JTT9; -.
DR   STRING; 393305.YE2747; -.
DR   EnsemblBacteria; CAL12781; CAL12781; YE2747.
DR   KEGG; yen:YE2747; -.
DR   PATRIC; fig|393305.7.peg.2920; -.
DR   eggNOG; COG0282; Bacteria.
DR   HOGENOM; CLU_020352_0_1_6; -.
DR   OMA; PLPWRYY; -.
DR   UniPathway; UPA00621; -.
DR   Proteomes; UP000000642; 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; Transferase.
FT   CHAIN           1..412
FT                   /note="Propionate kinase"
FT                   /id="PRO_0000398203"
SQ   SEQUENCE   412 AA;  45001 MW;  65504A14656F4F8E CRC64;
     MSGKIMAINA GSSSLKFQLF SMLNEQTGQH HEQVLCQGLI ERIGMDDAIF NLRVGDVQWR
     ETLPIADCRQ GAEHLLRALI EHNVIDSLDE IIGVGHRVAH GGETFADSVL ITPQVLDKIE
     QLGTLAPLHN PVNALGIRVF QLALPHASAV AVFDTAFHQT LSQTSFLYPL PWRYYEELGI
     RRYGFHGTSH KYVSAVCAER MGQPLAALRI VSCHLGNGSS ICAIGHGKSV NTSMGFTPQA
     GVMMGTRSGD IDPSILPFIQ QTEGKSAVEI NHLINNQSGL LGISGISHDY RDVEQAADNG
     NRRAALALEL FAERIRAVIG SYIVQLGGID ALIFTGGIGE NSRSARQQIC RELTFLGIEL
     DQEKNIRNQF FIQQDTAPVQ IAIVNTNEEL MIARDVLRVA LNLPVQPALA TQ