TDCD_EDWTE
ID TDCD_EDWTE Reviewed; 402 AA.
AC D0ZE10;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=ETAE_0896;
OS Edwardsiella tarda (strain EIB202).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=498217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EIB202;
RX PubMed=19865481; DOI=10.1371/journal.pone.0007646;
RA Wang Q., Yang M., Xiao J., Wu H., Wang X., Lv Y., Xu L., Zheng H., Wang S.,
RA Zhao G., Liu Q., Zhang Y.;
RT "Genome sequence of the versatile fish pathogen Edwardsiella tarda provides
RT insights into its adaptation to broad host ranges and intracellular
RT niches.";
RL PLoS ONE 4:E7646-E7646(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; CP001135; ACY83741.1; -; Genomic_DNA.
DR RefSeq; WP_012847761.1; NC_013508.1.
DR AlphaFoldDB; D0ZE10; -.
DR SMR; D0ZE10; -.
DR EnsemblBacteria; ACY83741; ACY83741; ETAE_0896.
DR KEGG; etr:ETAE_0896; -.
DR HOGENOM; CLU_020352_0_1_6; -.
DR OMA; IHYLYSI; -.
DR OrthoDB; 537106at2; -.
DR UniPathway; UPA00052; UER00510.
DR Proteomes; UP000002634; 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_0000398205"
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; 43094 MW; 9153733AD19DCFF0 CRC64;
MHEYPVVLVI NSGSSSIKFS VLDAQRCEVL LAGIAEGINS GSATLSVNGA APVALAQRGY
EPALAAICAE LEKRSLIDSV ALIGHRVAHG GNLFQQSAIV DDEVMEKIRR ISPLAPLHNY
ANLSGMVSAR HLFPGVTQVA VFDTSFHQTL APEAWLYALP YRYAQEYGVR RYGFHGTSHR
YVSQRAHHLL GLSEADSGLV IAHLGNGASI CAVRNGRSVD TSMGMTPLEG LMMGTRSGDV
DFGALAWIAS QTGQSIADLE QMVNTESGLL GISGLSSDLR VLERAQREGH QRADLAIRTF
VHRIARHIGG HAASLRRLDG IIFTGGIGEN SALIRRMVLE HLSVFGITLA PDKNNMPGSA
GERIISGEDS AVICAVIPTD EERMIALDAL RLGKIMPSIE YA
