ID Q466Q7_METBF Unreviewed; 253 AA. AC Q466Q7; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 90. DE RecName: Full=4-phosphopantoate--beta-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02224}; DE EC=6.3.2.36 {ECO:0000256|HAMAP-Rule:MF_02224}; DE AltName: Full=Phosphopantothenate synthetase {ECO:0000256|HAMAP-Rule:MF_02224}; DE Short=PPS {ECO:0000256|HAMAP-Rule:MF_02224}; GN OrderedLocusNames=Mbar_A3254 {ECO:0000313|EMBL:AAZ72135.1}; OS Methanosarcina barkeri (strain Fusaro / DSM 804). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=269797 {ECO:0000313|EMBL:AAZ72135.1}; RN [1] {ECO:0000313|EMBL:AAZ72135.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Fusaro {ECO:0000313|EMBL:AAZ72135.1}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Goodwin L.A., Saunders E.H., Schmutz J., RA Larimer F., Land M., Anderson I., Richardson P.; RT "Complete sequence of chromosome 1 of Methanosarcina barkeri str. fusaro."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the condensation of (R)-4-phosphopantoate and beta- CC alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway. CC {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_02224}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_02224}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02224}. CC -!- SIMILARITY: Belongs to the archaeal phosphopantothenate synthetase CC family. {ECO:0000256|HAMAP-Rule:MF_02224}. 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; CP000099; AAZ72135.1; -; Genomic_DNA. DR AlphaFoldDB; Q466Q7; -. DR STRING; 269797.Mbar_A3254; -. DR PaxDb; 269797-Mbar_A3254; -. DR KEGG; mba:Mbar_A3254; -. DR eggNOG; arCOG04262; Archaea. DR HOGENOM; CLU_078701_0_0_2; -. DR OrthoDB; 10078at2157; -. DR UniPathway; UPA00241; -. 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; Phosphopantoate/pantothenate synthetase; 1. DR HAMAP; MF_02224; PPS; 1. DR InterPro; IPR002855; PPS/PS. DR InterPro; IPR038138; PPS/PS_sf. DR NCBIfam; NF041123; phpantohe_syn_Arch; 1. DR PANTHER; PTHR40695; 4-PHOSPHOPANTOATE--BETA-ALANINE LIGASE; 1. DR PANTHER; PTHR40695:SF1; 4-PHOSPHOPANTOATE--BETA-ALANINE LIGASE; 1. DR Pfam; PF02006; PPS_PS; 1. DR PIRSF; PIRSF004853; UCP004853; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_02224}; KW Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993, ECO:0000256|HAMAP- KW Rule:MF_02224}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02224}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_02224}. FT BINDING 17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02224" FT BINDING 39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02224" FT BINDING 179..181 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02224" FT BINDING 185..186 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02224" FT BINDING 197..198 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02224" SQ SEQUENCE 253 AA; 27799 MW; D0E7942A1CDC00C4 CRC64; MTEIPKDHPR YESLLAREKV AAGVKMGITS VQGLISQGRG ESFDYLIGER STKSALYAER AAVAALLLAK NPVISVNGNA AVLAPDKIVA LADVTEAKLE VNLFHRTETR VHLIIEQLKA NGASEVLGKN PDVSLELSHA RRLVESRGIY SADVVLVPLE DGDRCEKLVE MGKTVIAIDL NPLSRTSKMA TISIVDNLTR ALENMIKFGV ELKKERNEEL VKLITTYDNK KVLIEAISEI QENLKAMTVE LEQ //