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TDCD_CITK8
ID   TDCD_CITK8              Reviewed;         402 AA.
AC   A8AQ07;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 84.
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=CKO_04515;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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=ABV15570.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000822; ABV15570.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_024130974.1; NC_009792.1.
DR   AlphaFoldDB; A8AQ07; -.
DR   SMR; A8AQ07; -.
DR   STRING; 290338.CKO_04515; -.
DR   EnsemblBacteria; ABV15570; ABV15570; CKO_04515.
DR   GeneID; 45138071; -.
DR   KEGG; cko:CKO_04515; -.
DR   HOGENOM; CLU_020352_0_1_6; -.
DR   OrthoDB; 537106at2; -.
DR   UniPathway; UPA00052; UER00510.
DR   Proteomes; UP000008148; 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   Reference proteome; Transferase.
FT   CHAIN           1..402
FT                   /note="Propionate kinase"
FT                   /id="PRO_0000398204"
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;  43512 MW;  130F1966E26417ED CRC64;
     MNEFPVVLVI NCGSSSIKFS VLDATHCDVL MAGIADGINS EDAFLSVNGG EPAKLAHHSY
     EGALKAIAFE LEKRNLIDSV ALIGHRIAHG GNIFTASAII TDEVIENIRR VSPLAPLHNY
     ANLSGIESAQ HLFPGVQQVA VFDTSFHQTM APEAYLYGLP WKYFEELGVR RYGFHGTSHR
     YVSQRAHDLL ALQEEDSGLV VAHLGNGASI CAVRNGQSVD TSMGMTPLEG LMMGTRSGDV
     DFGAMAWIAS ETNQTLGDME RVVNKESGLL GISGLSSDLR VLEKAWHEGH ERAQLAIKTF
     VHRIARHIAG HAASLHRLDG IIFTGGIGEN SVLIRRLVIE HLAVLGVKLD HEMNSLPNSH
     GERIISSKDT NVICAVIPTN EEKMIALDAI HLGKVNAPVE FA
 
 
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