PPS_THEON
ID PPS_THEON Reviewed; 261 AA.
AC B6YXQ1;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=4-phosphopantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_02224, ECO:0000305};
DE EC=6.3.2.36 {ECO:0000255|HAMAP-Rule:MF_02224};
DE AltName: Full=Phosphopantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_02224, ECO:0000303|PubMed:24021277};
DE Short=PPS {ECO:0000255|HAMAP-Rule:MF_02224, ECO:0000303|PubMed:24021277};
GN OrderedLocusNames=TON_1374 {ECO:0000312|EMBL:ACJ16864.1};
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
RN [2] {ECO:0007744|PDB:4MB0, ECO:0007744|PDB:4MB2}
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP ATP, AND SUBUNIT.
RC STRAIN=NA1;
RX PubMed=24021277; DOI=10.1016/j.bbrc.2013.09.008;
RA Kim M.K., An Y.J., Cha S.S.;
RT "The crystal structure of a novel phosphopantothenate synthetase from the
RT hyperthermophilic archaea, Thermococcus onnurineus NA1.";
RL Biochem. Biophys. Res. Commun. 439:533-538(2013).
CC -!- FUNCTION: Catalyzes the condensation of (R)-4-phosphopantoate and beta-
CC alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway.
CC {ECO:0000255|HAMAP-Rule:MF_02224}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4-phosphopantoate + ATP + beta-alanine = (R)-4'-
CC phosphopantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:27930,
CC ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:61294,
CC ChEBI:CHEBI:456215; EC=6.3.2.36; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02224};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02224}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02224,
CC ECO:0000269|PubMed:24021277}.
CC -!- SIMILARITY: Belongs to the archaeal phosphopantothenate synthetase
CC family. {ECO:0000255|HAMAP-Rule:MF_02224, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000855; ACJ16864.1; -; Genomic_DNA.
DR RefSeq; WP_012572336.1; NC_011529.1.
DR PDB; 4MB0; X-ray; 1.96 A; A/B/C/D=1-261.
DR PDB; 4MB2; X-ray; 2.19 A; A/B/C/D=1-261.
DR PDBsum; 4MB0; -.
DR PDBsum; 4MB2; -.
DR AlphaFoldDB; B6YXQ1; -.
DR SMR; B6YXQ1; -.
DR STRING; 523850.TON_1374; -.
DR EnsemblBacteria; ACJ16864; ACJ16864; TON_1374.
DR GeneID; 7018405; -.
DR KEGG; ton:TON_1374; -.
DR PATRIC; fig|523850.10.peg.1382; -.
DR eggNOG; arCOG04262; Archaea.
DR HOGENOM; CLU_078701_0_0_2; -.
DR OMA; PKSHPRY; -.
DR OrthoDB; 76877at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000002727; Chromosome.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.12640; -; 1.
DR HAMAP; MF_02224; PPS; 1.
DR InterPro; IPR002855; PPS/PS.
DR InterPro; IPR038138; PPS/PS_sf.
DR PANTHER; PTHR40695; PTHR40695; 1.
DR Pfam; PF02006; PPS_PS; 1.
DR PIRSF; PIRSF004853; UCP004853; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Ligase;
KW Nucleotide-binding.
FT CHAIN 1..261
FT /note="4-phosphopantoate--beta-alanine ligase"
FT /id="PRO_0000448252"
FT BINDING 17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02224,
FT ECO:0000269|PubMed:24021277, ECO:0007744|PDB:4MB2"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02224,
FT ECO:0000269|PubMed:24021277, ECO:0007744|PDB:4MB2"
FT BINDING 181..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24021277,
FT ECO:0007744|PDB:4MB2"
FT BINDING 187..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
FT BINDING 199..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02224,
FT ECO:0000269|PubMed:24021277, ECO:0007744|PDB:4MB2"
FT HELIX 11..25
FT /evidence="ECO:0007829|PDB:4MB0"
FT HELIX 31..47
FT /evidence="ECO:0007829|PDB:4MB0"
FT HELIX 53..68
FT /evidence="ECO:0007829|PDB:4MB0"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:4MB0"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:4MB0"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:4MB0"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4MB0"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:4MB0"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:4MB0"
FT TURN 148..153
FT /evidence="ECO:0007829|PDB:4MB0"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:4MB0"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:4MB0"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:4MB0"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:4MB0"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:4MB0"
FT HELIX 200..214
FT /evidence="ECO:0007829|PDB:4MB0"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:4MB0"
FT HELIX 231..252
FT /evidence="ECO:0007829|PDB:4MB0"
SQ SEQUENCE 261 AA; 29685 MW; 8697C5645653A96F CRC64;
MVKIPKSHPR YWSLYYREKI IEGMEKGMTA KAGLIAHGRG EAFDYLIGER TIEPAERAMR
AAVAKLLLAE NPVVSVNGNV AALVPKETIE LARALNAKLE INLFYRTEDR VKAIAEELRK
YDPEIELLGI NPTKRIPGLE HERGKVDENG IWKADVVVVP LEDGDRTEAL VRMGKFVITI
DLNPLSRSAR MADITIVDNI VRAYPRMTEL AREMKDYSRG ELIRIIEEYD NGKTLNDVLL
HIRDRLTKLA EGGIWRKKQL D
