ID M0K7V5_9EURY Unreviewed; 249 AA. AC M0K7V5; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 19-JAN-2022, entry version 24. 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 ORFNames=C436_02457 {ECO:0000313|EMBL:EMA15910.1}; OS Haloarcula sinaiiensis ATCC 33800. OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales; OC Haloarculaceae; Haloarcula. OX NCBI_TaxID=662476 {ECO:0000313|EMBL:EMA15910.1, ECO:0000313|Proteomes:UP000011659}; RN [1] {ECO:0000313|EMBL:EMA15910.1, ECO:0000313|Proteomes:UP000011659} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33800 {ECO:0000313|EMBL:EMA15910.1, RC ECO:0000313|Proteomes:UP000011659}; RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784; RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D., RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.; RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals RT strategies for static and dynamic osmo-response."; RL PLoS Genet. 10:E1004784-E1004784(2014). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EMA15910.1}. 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; AOLR01000003; EMA15910.1; -; Genomic_DNA. DR RefSeq; WP_004957867.1; NZ_AOLR01000003.1. DR EnsemblBacteria; EMA15910; EMA15910; C436_02457. DR GeneID; 64821654; -. DR PATRIC; fig|662476.7.peg.489; -. DR OrthoDB; 76877at2157; -. DR UniPathway; UPA00241; -. DR Proteomes; UP000011659; Unassembled WGS sequence. 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02224}; KW Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_02224}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02224}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02224}. FT NP_BIND 183..185 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02224" FT NP_BIND 189..190 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02224" FT NP_BIND 201..202 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02224" FT BINDING 20 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02224" FT BINDING 42 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02224" SQ SEQUENCE 249 AA; 26723 MW; 46381A69F12ED408 CRC64; MSEDVDLPES HPRYESLLTR HRIEAGVDRG ITSRQGLIAQ GRGEAFDYLL GERTIDSADD AERAAAAHLL SADHAVVSVN GNAAALVPGE LVELAEVTGA DLEVNLFNRT EERIEAIAEY LREHGATDVR GLTADGRIPG LDHERAKVDA DGIGAADVVL VPLEDGDRAE ALGEMGKTEL VIDLNPRSRS AEVATVPIID NIIRAIPNIT EHARDLRGDP DAQQDAIDTF DADSALTAAE RTIREGDLE //