ID   PDUW_TOLAT              Reviewed;         392 AA.
AC   C4LFE6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=Tola_1703;
OS   Tolumonas auensis (strain DSM 9187 / TA4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Tolumonas.
OX   NCBI_TaxID=595494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9187 / TA4;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA   Beller H.;
RT   "Complete sequence of Tolumonas auensis DSM 9187.";
RL   Submitted (MAY-2009) 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; CP001616; ACQ93313.1; -; Genomic_DNA.
DR   RefSeq; WP_015878784.1; NC_012691.1.
DR   AlphaFoldDB; C4LFE6; -.
DR   SMR; C4LFE6; -.
DR   STRING; 595494.Tola_1703; -.
DR   EnsemblBacteria; ACQ93313; ACQ93313; Tola_1703.
DR   KEGG; tau:Tola_1703; -.
DR   eggNOG; COG0282; Bacteria.
DR   HOGENOM; CLU_020352_0_1_6; -.
DR   OMA; PLHNPME; -.
DR   OrthoDB; 537106at2; -.
DR   UniPathway; UPA00621; -.
DR   Proteomes; UP000009073; 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..392
FT                   /note="Propionate kinase"
FT                   /id="PRO_0000398202"
SQ   SEQUENCE   392 AA;  42970 MW;  376BAEA04E7DEC5F CRC64;
     MLQKIMAINA GSSSLKFQLF SMPDEQVITK GMIERIGKQD AFFSIQYGEQ KHRETFAVEN
     HQQAVDHLLS ALLDHEIIKS LDEIAGVGHR VAHGGEAFSD SACIDAAALQ QIEHLGTLAP
     LHNPVNAIGI RAFMEALPHA KAVAVFDTSF HQTMPPETFL YALPYRYYQE QGIRRYGFHG
     TSHKYVSQIC AEKMETPLSD LRLISCHLGN GSSLCAIQHG RSVNTSMGFT PLAGVMMGTR
     CGDIDPSIMP YLAKQENKTA DELNALINNE SGLLGISGVS NDYRDVEQAA KEGNERAQLA
     LKMFAERIRS FIGSYIAHMG GLDALIFTGG IGENSRTARA AICHALEYLG IALDETKNNA
     NETFIQQDSG PVKIAVINTN EELMIARDVM RV