ID PANC_AKKM8 Reviewed; 281 AA. AC B2UND0; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 10-FEB-2021, entry version 73. DE RecName: Full=Pantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_00158}; DE Short=PS {ECO:0000255|HAMAP-Rule:MF_00158}; DE EC=6.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00158}; DE AltName: Full=Pantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00158}; DE AltName: Full=Pantoate-activating enzyme {ECO:0000255|HAMAP-Rule:MF_00158}; GN Name=panC {ECO:0000255|HAMAP-Rule:MF_00158}; OrderedLocusNames=Amuc_0404; OS Akkermansia muciniphila (strain ATCC BAA-835 / Muc). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Akkermansiaceae; Akkermansia. OX NCBI_TaxID=349741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-835 / Muc; RX PubMed=21390229; DOI=10.1371/journal.pone.0016876; RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M., RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.; RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin RT degrader, and its use in exploring intestinal metagenomes."; RL PLoS ONE 6:E16876-E16876(2011). CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in CC an ATP-dependent reaction via a pantoyl-adenylate intermediate. CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00158}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)- CC pantothenate from (R)-pantoate and beta-alanine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong CC mechanism. {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- SIMILARITY: Belongs to the pantothenate synthetase family. CC {ECO:0000255|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; CP001071; ACD04242.1; -; Genomic_DNA. DR RefSeq; WP_012419457.1; NC_010655.1. DR SMR; B2UND0; -. DR STRING; 349741.Amuc_0404; -. DR EnsemblBacteria; ACD04242; ACD04242; Amuc_0404. DR KEGG; amu:Amuc_0404; -. DR eggNOG; COG0414; Bacteria. DR HOGENOM; CLU_047148_0_0_0; -. DR OMA; CNHKLEP; -. DR OrthoDB; 1661843at2; -. DR BioCyc; AMUC349741:G1GBX-447-MONOMER; -. DR UniPathway; UPA00028; UER00005. DR Proteomes; UP000001031; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule. 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; Cytoplasm; Ligase; Nucleotide-binding; KW Pantothenate biosynthesis; Reference proteome. FT CHAIN 1..281 FT /note="Pantothenate synthetase" FT /id="PRO_1000097026" FT NP_BIND 30..37 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT NP_BIND 150..153 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT NP_BIND 187..190 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT ACT_SITE 37 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 64 FT /note="Beta-alanine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 64 FT /note="Pantoate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 156 FT /note="Pantoate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" FT BINDING 179 FT /note="ATP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158" SQ SEQUENCE 281 AA; 30917 MW; CC39BF5AD725D307 CRC64; MQTFSTKAQL RAALLKHHRK HDHVVLVPTM GALHAGHRAL LEQARKLAGE DGVVVASIFV NPIQFNNSSD LQTYPRTPEK DLEVCEGAGV DYVFSPAPEE MYSGERSIAV EESFLSATLC GASRPGHFSG VCTVLAKLFN LVQPTDAIFG KKDYQQLAII RRMVRDLDFP VRIHGAEIVR HGNGLAYSSR NARLTPEQKE QAVVIRQAML QARDEFQAGA DASKVKEHAA AMIEGVPGTR IDYLEIVDAE TMQPVAENRK PALMAAAVYF GDVRLIDNIE L //