ID A0A7R7TQ53_THETH Unreviewed; 276 AA. AC A0A7R7TQ53; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-SEP-2021, entry version 2. DE RecName: Full=Pantothenate synthetase {ECO:0000256|HAMAP-Rule:MF_00158}; DE Short=PS {ECO:0000256|HAMAP-Rule:MF_00158}; DE EC=6.3.2.1 {ECO:0000256|HAMAP-Rule:MF_00158}; DE AltName: Full=Pantoate--beta-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00158}; DE AltName: Full=Pantoate-activating enzyme {ECO:0000256|HAMAP-Rule:MF_00158}; GN Name=panC {ECO:0000256|HAMAP-Rule:MF_00158, GN ECO:0000313|EMBL:BCQ01238.1}; GN ORFNames=TthHB5002_20100 {ECO:0000313|EMBL:BCP98907.1}, GN TthHB5008_20080 {ECO:0000313|EMBL:BCQ01238.1}; OS Thermus thermophilus. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=274 {ECO:0000313|EMBL:BCQ01238.1}; RN [1] {ECO:0000313|EMBL:BCQ01238.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HB5002 {ECO:0000313|EMBL:BCP98907.1}, and HB5008 RC {ECO:0000313|EMBL:BCQ01238.1}; RA Miyazaki K., Moriya T., Oshima T., Yura K., Bessho Y.; RT "Complete genome sequences of twin Thermus thermophilus strains HB5002 and RT HB5008 isolated from Mine Onsen hot spring in Japan."; RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in CC an ATP-dependent reaction via a pantoyl-adenylate intermediate. CC {ECO:0000256|HAMAP-Rule:MF_00158}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + CC diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1; CC Evidence={ECO:0000256|ARBA:ARBA00001155, ECO:0000256|HAMAP- CC Rule:MF_00158}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)- CC pantothenate from (R)-pantoate and beta-alanine: step 1/1. CC {ECO:0000256|ARBA:ARBA00004990, ECO:0000256|HAMAP-Rule:MF_00158}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00158}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00158}. CC -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong CC mechanism. {ECO:0000256|HAMAP-Rule:MF_00158}. CC -!- SIMILARITY: Belongs to the pantothenate synthetase family. CC {ECO:0000256|ARBA:ARBA00009256, ECO:0000256|HAMAP-Rule:MF_00158}. 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; AP024301; BCP98907.1; -; Genomic_DNA. DR EMBL; AP024305; BCQ01238.1; -; Genomic_DNA. DR UniPathway; UPA00028; UER00005. DR CDD; cd00560; PanC; 1. DR Gene3D; 3.30.1300.10; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00158; PanC; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR003721; Pantoate_ligase. DR InterPro; IPR042176; Pantoate_ligase_C. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR21299:SF1; PTHR21299:SF1; 1. DR Pfam; PF02569; Pantoate_ligase; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. DR TIGRFAMs; TIGR00018; panC; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00158}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00158}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00158}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00158}; KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655, KW ECO:0000256|HAMAP-Rule:MF_00158}. FT NP_BIND 25..32 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00158" FT NP_BIND 143..146 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00158" FT NP_BIND 180..183 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00158" FT ACT_SITE 32 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00158" FT BINDING 56 FT /note="Beta-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00158" FT BINDING 56 FT /note="Pantoate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00158" FT BINDING 149 FT /note="Pantoate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00158" FT BINDING 172 FT /note="ATP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00158" SQ SEQUENCE 276 AA; 30623 MW; E6396B80D0EF1917 CRC64; MRTVSTVAEL RAALPREGVG FVPTMGYLHR GHLALVERAR RENPFVVVSV FVNPLQFGPG EDYHRYPRDL ERDRALLQEA GVDLLFAPGV EEMYPGGFAT RVQVEGPLTA LWEGAVRPGH FQGVATVVAR LFLLVQPQRA YFGEKDYQQL LVVRRMVRDL GFPVEVVGVP TVREEDGLAL SSRNVYLSPE TRKKAPVLYR ALLAMREVAG QGGSVAEALR AGEEALRAVP EFRKDYLAIV HPETLLPLSD WVAGARGIVA GRFPEARLID NLEVYP //