ID   PDUW_CITK8              Reviewed;         404 AA.
AC   A8AEL8;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 77.
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=CKO_00779;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) 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:B1VB81, 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABV11931.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000822; ABV11931.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_024130206.1; NC_009792.1.
DR   AlphaFoldDB; A8AEL8; -.
DR   SMR; A8AEL8; -.
DR   STRING; 290338.CKO_00779; -.
DR   EnsemblBacteria; ABV11931; ABV11931; CKO_00779.
DR   GeneID; 45134978; -.
DR   KEGG; cko:CKO_00779; -.
DR   HOGENOM; CLU_020352_0_1_6; -.
DR   OrthoDB; 537106at2; -.
DR   UniPathway; UPA00621; -.
DR   Proteomes; UP000008148; 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_0000398196"
SQ   SEQUENCE   404 AA;  43961 MW;  2EC2E24CD33270D4 CRC64;
     MSHKIMAINA GSSSLKFQLL AMPQGEMICQ GLIERIGMAN ARVTMKTSAQ KWQETAPIAD
     HRESVTLLLD KLLSHHIINT LQDIDGVGHR VAHGGEFFKD SARVTDETLA QIERLAELAP
     LHNPVNALGI HIFRQLLPST PSVAVFDTAF HQTLDESAYI YPLPWRYYTE LGIRRYGFHG
     TSHKYVSTAL AERLGVPLSA LRVICCHLGN GSSICAIKGG QSVNTSMGFT PQSGVMMGTR
     SGDIDPSILP WIAEREGKTP QQLNYLLNNE SGLLGISGVS HDYRDVEQAA DGGNRRAALA
     LTLFAERIRA TIGSYIMQMG GLDALIFTGG IGENSARARA AVCHNLHFLG LSIDEEKNLR
     NATFIQAENA VVKVAVINTN EELMIAQDVM RIALSDKVTF GVSA