TDCD_ECOLI
ID TDCD_ECOLI Reviewed; 402 AA.
AC P11868; P76666; Q2M992;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 03-AUG-2022, entry version 174.
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}; Synonyms=yhaA;
GN OrderedLocusNames=b3115, JW5806;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-331.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2660107; DOI=10.1093/nar/17.10.3994;
RA Schweizer H., Datta P.;
RT "The complete nucleotide sequence of the tdc region of Escherichia coli.";
RL Nucleic Acids Res. 17:3994-3994(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-331.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=3053659; DOI=10.1128/jb.170.11.5352-5359.1988;
RA Goss T.J., Schweizer H.P., Datta P.;
RT "Molecular characterization of the tdc operon of Escherichia coli K-12.";
RL J. Bacteriol. 170:5352-5359(1988).
RN [5]
RP IDENTIFICATION.
RX PubMed=8226682; DOI=10.1128/jb.175.22.7348-7355.1993;
RA Grundy F.J., Waters D.A., Allen S.H.G., Henkin T.M.;
RT "Regulation of the Bacillus subtilis acetate kinase gene by CcpA.";
RL J. Bacteriol. 175:7348-7355(1993).
RN [6]
RP FUNCTION AS A PROPIONATE KINASE AND IN THREONINE CATABOLISM, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=9484901; DOI=10.1046/j.1365-2958.1998.00696.x;
RA Hesslinger C., Fairhurst S.A., Sawers G.;
RT "Novel keto acid formate-lyase and propionate kinase enzymes are components
RT of an anaerobic pathway in Escherichia coli that degrades L-threonine to
RT propionate.";
RL Mol. Microbiol. 27:477-492(1998).
CC -!- FUNCTION: Catalyzes the conversion of propionyl phosphate and ADP to
CC propionate and ATP. It can also use acetyl phosphate as phosphate group
CC acceptor. {ECO:0000255|HAMAP-Rule:MF_01881,
CC ECO:0000269|PubMed:9484901}.
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 -!- INTERACTION:
CC P11868; P37747: glf; NbExp=2; IntAct=EBI-553884, EBI-558730;
CC -!- SIMILARITY: Belongs to the acetokinase family. TdcD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01881}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24663.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA57919.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA32595.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA57919.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76150.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77164.1; -; Genomic_DNA.
DR EMBL; X14430; CAA32595.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M23638; AAA24663.1; ALT_FRAME; Genomic_DNA.
DR PIR; H65100; Q3ECTD.
DR RefSeq; NP_417585.2; NC_000913.3.
DR RefSeq; WP_001295545.1; NZ_LN832404.1.
DR AlphaFoldDB; P11868; -.
DR SMR; P11868; -.
DR BioGRID; 4262417; 22.
DR DIP; DIP-10971N; -.
DR IntAct; P11868; 3.
DR STRING; 511145.b3115; -.
DR PaxDb; P11868; -.
DR PRIDE; P11868; -.
DR EnsemblBacteria; AAC76150; AAC76150; b3115.
DR EnsemblBacteria; BAE77164; BAE77164; BAE77164.
DR GeneID; 947635; -.
DR KEGG; ecj:JW5806; -.
DR KEGG; eco:b3115; -.
DR PATRIC; fig|511145.12.peg.3209; -.
DR EchoBASE; EB1159; -.
DR eggNOG; COG0282; Bacteria.
DR HOGENOM; CLU_020352_0_1_6; -.
DR InParanoid; P11868; -.
DR PhylomeDB; P11868; -.
DR BioCyc; EcoCyc:PROPKIN-MON; -.
DR BioCyc; MetaCyc:PROPKIN-MON; -.
DR UniPathway; UPA00052; UER00510.
DR PRO; PR:P11868; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008776; F:acetate kinase activity; IDA:EcoCyc.
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; IDA:EcoCyc.
DR GO; GO:0006083; P:acetate metabolic process; IBA:GO_Central.
DR GO; GO:0019665; P:anaerobic amino acid catabolic process; IDA:EcoCyc.
DR GO; GO:0070689; P:L-threonine catabolic process to propionate; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR GO; GO:0006567; P:threonine catabolic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..402
FT /note="Propionate kinase"
FT /id="PRO_0000107652"
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"
FT CONFLICT 121
FT /note="A -> P (in Ref. 3; CAA32595 and 4; AAA24663)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="V -> L (in Ref. 3; CAA32595 and 4; AAA24663)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="G -> A (in Ref. 3; CAA32595 and 4; AAA24663)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="A -> P (in Ref. 3; CAA32595 and 4; AAA24663)"
FT /evidence="ECO:0000305"
FT CONFLICT 249..250
FT /note="AS -> RR (in Ref. 3; CAA32595 and 4; AAA24663)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="L -> H (in Ref. 3; CAA32595 and 4; AAA24663)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="E -> G (in Ref. 3; CAA32595 and 4; AAA24663)"
FT /evidence="ECO:0000305"
FT CONFLICT 396..402
FT /note="NAPAEFA -> KEGANKRGNSSRLTQSFHFFMFEPIFSPVNALNQPI (in
FT Ref. 2; BAE77164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 43384 MW; 2E49756262C77144 CRC64;
MNEFPVVLVI NCGSSSIKFS VLDASDCEVL MSGIADGINS ENAFLSVNGG EPAPLAHHSY
EGALKAIAFE LEKRNLNDSV ALIGHRIAHG GSIFTESAII TDEVIDNIRR VSPLAPLHNY
ANLSGIESAQ QLFPGVTQVA VFDTSFHQTM APEAYLYGLP WKYYEELGVR RYGFHGTSHR
YVSQRAHSLL NLAEDDSGLV VAHLGNGASI CAVRNGQSVD TSMGMTPLEG LMMGTRSGDV
DFGAMSWVAS QTNQSLGDLE RVVNKESGLL GISGLSSDLR VLEKAWHEGH ERAQLAIKTF
VHRIARHIAG HAASLRRLDG IIFTGGIGEN SSLIRRLVME HLAVLGLEID TEMNNRSNSC
GERIVSSENA RVICAVIPTN EEKMIALDAI HLGKVNAPAE FA
