PDUW_KLEP3
ID PDUW_KLEP3 Reviewed; 404 AA.
AC B5XUR6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=KPK_0893;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI07162.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XUR6; -.
DR SMR; B5XUR6; -.
DR EnsemblBacteria; ACI07162; ACI07162; KPK_0893.
DR KEGG; kpe:KPK_0893; -.
DR HOGENOM; CLU_020352_0_1_6; -.
DR OMA; PLPWRYY; -.
DR OrthoDB; 537106at2; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000001734; 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..404
FT /note="Propionate kinase"
FT /id="PRO_0000398199"
SQ SEQUENCE 404 AA; 43760 MW; DBFC6732B606AC03 CRC64;
MTYKIMAINA GSSSLKFQLL NMPQGALLCQ GLIERIGLPE ARFMLKTSAQ KWQETLPIAD
HHEAVTLLLE ALTGRGILSS LQEIDGVGHR VAHGGERFKD AALVCDDTLR EIERLAELAP
LHNPVNALGI RLFRQRLPAV PAVAVFDTAF HQTLAPEAWL YPLPWRYYAE LGIRRYGFHG
TSHHYVSSAL AEKLGVPLSA LRVVSCHLGN GCSVCAIKGG QSVNTSMGFT PQSGVMMGTR
SGDIDPSILP WLVEKEGKSA LQLSQLLNNE SGLLGVSGVS SDYRDVEQAA DAGNERAALA
LSLFAERIRA TIGSYIMQMG GLDALIFTGG IGEHSARARA TICRNLHFLG LALDDEKNQR
SATFIQADNA LVKVAVINTN EELMIARDVM RLALPQAREL TVSA