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TDCD_ECOL6
ID   TDCD_ECOL6              Reviewed;         402 AA.
AC   P59244;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=c3873;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN82314.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN82314.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001298325.1; NC_004431.1.
DR   AlphaFoldDB; P59244; -.
DR   SMR; P59244; -.
DR   STRING; 199310.c3873; -.
DR   EnsemblBacteria; AAN82314; AAN82314; c3873.
DR   KEGG; ecc:c3873; -.
DR   eggNOG; COG0282; Bacteria.
DR   HOGENOM; CLU_209227_0_0_6; -.
DR   OMA; IHYLYSI; -.
DR   UniPathway; UPA00052; UER00510.
DR   Proteomes; UP000001410; 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_0000107654"
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;  43421 MW;  2B8321EE4BC8B5B8 CRC64;
     MNEFPVVLVI NCGSSSIKFS VLNASDCEVL MSGIADGINS ENAFLSVNGG EPAPLAHHSY
     EGALKAIAFE LEKRNLNDNV ALIGHRIAHG GSIFTESAII TDEVIDNIRR VSPLAPLHNY
     ANLSGIESAQ QLFPGVTQVA VFDTSFHQTM APEAYLYGLP WKYYEELGVR RYGFHGTSHR
     YVSQRAHSLL NLAEDDSGLV VAHLGNGASI CAVRNGQSVD TSMGMTPLEG LMMGTRSGDV
     DFGAMSWVAS QTNQSLGDLE RVVNKESGLL GISGLSSDLR VLEKAWHEGH ERAQLAIKTF
     VHRIARHIAG HAASLHRLDG IIFTGGIGEN SSLIRRLVME HLAVLGVEID TEMNNRSNSF
     GERIVSSENA RVICAVIPTN EEKMIALDAI HLGKVNAPAE FA
 
 
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