PPS_METMA
ID PPS_METMA Reviewed; 253 AA.
AC Q8PUQ1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=4-phosphopantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_02224};
DE EC=6.3.2.36 {ECO:0000255|HAMAP-Rule:MF_02224};
DE AltName: Full=Phosphopantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_02224};
DE Short=PPS {ECO:0000255|HAMAP-Rule:MF_02224};
GN OrderedLocusNames=MM_2281;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP PRELIMINARY FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=18422645; DOI=10.1111/j.1742-4658.2008.06416.x;
RA Ronconi S., Jonczyk R., Genschel U.;
RT "A novel isoform of pantothenate synthetase in the Archaea.";
RL FEBS J. 275:2754-2764(2008).
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:18422645}.
CC -!- MISCELLANEOUS: Was originally thought to have pantothenate synthetase
CC (PS) activity. Purified recombinant protein shows no PS activity on its
CC own, but the enzyme enables substantial synthesis of 4'-
CC phosphopantothenate from beta-alanine, pantoate and ATP when coupled
CC with E. coli pantothenate kinase. ADP, but not AMP, was detected as a
CC coproduct of the coupled reaction. {ECO:0000305|PubMed:18422645}.
CC -!- SIMILARITY: Belongs to the archaeal phosphopantothenate synthetase
CC family. {ECO:0000255|HAMAP-Rule:MF_02224, ECO:0000305}.
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DR EMBL; AE008384; AAM31977.1; -; Genomic_DNA.
DR RefSeq; WP_011034208.1; NC_003901.1.
DR AlphaFoldDB; Q8PUQ1; -.
DR SMR; Q8PUQ1; -.
DR STRING; 192952.MM_2281; -.
DR EnsemblBacteria; AAM31977; AAM31977; MM_2281.
DR GeneID; 44087653; -.
DR GeneID; 66136221; -.
DR KEGG; mma:MM_2281; -.
DR PATRIC; fig|192952.21.peg.2615; -.
DR eggNOG; arCOG04262; Archaea.
DR HOGENOM; CLU_078701_0_0_2; -.
DR OMA; PKSHPRY; -.
DR BRENDA; 6.3.2.44; 3270.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000000595; 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 ATP-binding; Coenzyme A biosynthesis; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..253
FT /note="4-phosphopantoate--beta-alanine ligase"
FT /id="PRO_0000401205"
FT BINDING 17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
FT BINDING 179..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
FT BINDING 185..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
FT BINDING 197..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
SQ SEQUENCE 253 AA; 27594 MW; 1848DBFBDB05F72A CRC64;
MTDIPHDHPR YESLLAREKV AAGVKMGITS IQGLIAQGRG ESFDYLIGER STESALYAER
AAVAALLLAE NPVISVNGNV AALAPDKVVT LADITGARIE VNLFHRTDTR VHLIIEQLKA
SGAAEVLGKN PDASLELSHD RRLVSSKGIY TADVVLVPLE DGDRCEKLVE MGKTVITIDL
NPLSRTSKTA TISIVDNLTR ALGNMAKFAQ EMKKERKEEL VKLITTYDNK RTLSEAISEI
QEHLKTMAAE TGY
