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 16-MAY-2012, entry version 28. DE RecName: Full=Pantothenate synthetase; DE Short=PS; DE EC=6.3.2.1; DE AltName: Full=Pantoate--beta-alanine ligase; DE AltName: Full=Pantoate-activating enzyme; GN Name=panC; OrderedLocusNames=Amuc_0404; OS Akkermansia muciniphila (strain ATCC BAA-835). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Verrucomicrobiaceae; Akkermansia. OX NCBI_TaxID=349741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-835; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Smidt H., Derrien M., Plugge C.M., Zoetendal E.G., RA de Vos W.M., Richardson P.; RT "Complete sequence of Akkermansia muciniphila ATCC BAA-835."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine CC in an ATP-dependent reaction via a pantoyl-adenylate intermediate CC (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantoate + beta-alanine = AMP + CC diphosphate + (R)-pantothenate. CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; CC (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong CC mechanism (By similarity). CC -!- SIMILARITY: Belongs to the pantothenate synthetase family. 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; YP_001877023.1; NC_010655.1. DR ProteinModelPortal; B2UND0; -. DR STRING; B2UND0; -. DR GeneID; 6274820; -. DR GenomeReviews; CP001071_GR; Amuc_0404. DR KEGG; amu:Amuc_0404; -. DR PATRIC; 20833404; VBIAkkMuc16855_0458. DR eggNOG; COG0414; -. DR HOGENOM; HOG000175516; -. DR KO; K01918; -. DR OMA; LNMPIQI; -. 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:EC. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR HAMAP; MF_00158; PanC; 1; -. DR InterPro; IPR004821; Cyt_trans-rel. DR InterPro; IPR003721; Pantoate_ligase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR21299:SF1; Pantoate_ligase; 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; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Pantothenate biosynthesis. FT CHAIN 1 281 Pantothenate synthetase. FT /FTId=PRO_1000097026. FT NP_BIND 30 37 ATP (By similarity). FT NP_BIND 150 153 ATP (By similarity). FT NP_BIND 187 190 ATP (By similarity). FT ACT_SITE 37 37 Proton donor (By similarity). FT BINDING 64 64 Beta-alanine (By similarity). FT BINDING 64 64 Pantoate (By similarity). FT BINDING 156 156 Pantoate (By similarity). FT BINDING 179 179 ATP; via amide nitrogen and carbonyl FT oxygen (By similarity). 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 //