TDCD_SALA4
ID TDCD_SALA4 Reviewed; 402 AA.
AC B5F6P9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=SeAg_B3430;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001138; ACH48886.1; -; Genomic_DNA.
DR RefSeq; WP_001001854.1; NC_011149.1.
DR AlphaFoldDB; B5F6P9; -.
DR SMR; B5F6P9; -.
DR EnsemblBacteria; ACH48886; ACH48886; SeAg_B3430.
DR KEGG; sea:SeAg_B3430; -.
DR HOGENOM; CLU_020352_0_1_6; -.
DR OMA; IHYLYSI; -.
DR UniPathway; UPA00052; UER00510.
DR Proteomes; UP000008819; 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_0000398208"
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; 43689 MW; 40900336AD32A214 CRC64;
MNEFPVVLVI NCGSSSIKFS VLDVATCDVL MAGIADGMNT ENAFLSINGD KPINLAHSNY
EDALKAIAFE LEKRDLTDSV ALIGHRIAHG GELFTQSVII TDEIIDNIRR VSPLAPLHNY
ANLSGIDAAR HLFPAVRQVA VFDTSFHQTL APEAYLYGLP WEYFSSLGVR RYGFHGTSHR
YVSRRAYELL DLDEKNSGLI VAHLGNGASI CAVRNGQSVD TSMGMTPLEG LMMGTRSGDV
DFGAMAWIAK ETGQTLSDLE RVVNKESGLL GISGLSSDLR VLEKAWHEGH ERARLAIKTF
VHRIARHIAG HAASLHRLDG IIFTGGIGEN SVLIRQLAIE HLGVLGLTLD VEMNKQPNSH
GERIISANPS QVICAVIPTN EEKMIALDAI HLGNVKAPVE FA
