TDCD_SALTD
ID TDCD_SALTD Reviewed; 402 AA.
AC C9XHG0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Propionate kinase {ECO:0000255|HAMAP-Rule:MF_01881};
DE EC=2.7.2.15 {ECO:0000255|HAMAP-Rule:MF_01881};
GN Name=tdcD {ECO:0000255|HAMAP-Rule:MF_01881}; OrderedLocusNames=STMMW_32421;
OS Salmonella typhimurium (strain D23580).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=568708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D23580;
RX PubMed=19901036; DOI=10.1101/gr.091017.109;
RA Kingsley R.A., Msefula C.L., Thomson N.R., Kariuki S., Holt K.E.,
RA Gordon M.A., Harris D., Clarke L., Whitehead S., Sangal V., Marsh K.,
RA Achtman M., Molyneux M.E., Cormican M., Parkhill J., Maclennan C.A.,
RA Heyderman R.S., Dougan G.;
RT "Epidemic multiple drug resistant Salmonella typhimurium causing invasive
RT disease in sub-Saharan Africa have a distinct genotype.";
RL Genome Res. 19:2279-2287(2009).
CC -!- FUNCTION: Catalyzes the conversion of propionyl phosphate and ADP to
CC propionate and ATP. {ECO:0000255|HAMAP-Rule:MF_01881}.
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_01881};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01881};
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via propanoate
CC pathway; propanoate from L-threonine: step 4/4. {ECO:0000255|HAMAP-
CC Rule:MF_01881}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01881}.
CC -!- SIMILARITY: Belongs to the acetokinase family. TdcD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01881}.
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DR EMBL; FN424405; CBG26245.1; -; Genomic_DNA.
DR RefSeq; WP_001001853.1; NC_016854.1.
DR AlphaFoldDB; C9XHG0; -.
DR SMR; C9XHG0; -.
DR KEGG; sev:STMMW_32421; -.
DR PATRIC; fig|568708.3.peg.3456; -.
DR HOGENOM; CLU_020352_0_1_6; -.
DR OMA; IHYLYSI; -.
DR BioCyc; SENT568708:STMMW_RS16785-MON; -.
DR UniPathway; UPA00052; UER00510.
DR Proteomes; UP000002622; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008980; F:propionate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070689; P:L-threonine catabolic process to propionate; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00020; Acetate_kinase; 1.
DR HAMAP; MF_01881; Propion_kin_subfam1; 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; IPR024917; Propionate_kinase.
DR PANTHER; PTHR21060; PTHR21060; 1.
DR PANTHER; PTHR21060:SF17; PTHR21060:SF17; 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; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..402
FT /note="Propionate kinase"
FT /id="PRO_0000398209"
FT ACT_SITE 143
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01881"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01881"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01881"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01881"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01881"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01881"
FT BINDING 203..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01881"
FT BINDING 278..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01881"
FT BINDING 326..330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01881"
FT SITE 175
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01881"
FT SITE 236
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01881"
SQ SEQUENCE 402 AA; 43718 MW; EF387E43054FCAB3 CRC64;
MNEFPVVLVI NCGSSSIKFS VLDVATCDVL MAGIADGMNT ENAFLSINGD KPINLAHSNY
EDALKAIAFE LEKRDLTDSV ALIGHRIAHG GELFTQSVII TDEIIDNIRR VSPLAPLHNY
ANLSGIDAAR HLFPAVRQVA VFDTSFHQTL APEAYLYGLP WEYFSSLGVR RYGFHGTSHR
YVSRRAYELL DLDEKDSGLI VAHLGNGASI CAVRNGQSVD TSMGMTPLEG LMMGTRSGDV
DFGAMAWIAK ETGQTLSDLE RVVNKESGLL GISGLSSDLR VLEKAWHEGH ERARLAIKTF
VHRIARHIAG HAASLHRLDG IIFTGGIGEN SVLIRQLVIE HLGVLGLTLD VEMNKQPNSH
GERIISANPS QVICAVIPTN EEKMIALDAI HLGNVKAPVE FA
