ID   PANC_BUCAP              Reviewed;         285 AA.
AC   Q8K9U7;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 39.
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=BUsg_190;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; pantothenate biosynthesis;
CC       pantothenate from beta-alanine and pantoate: 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.
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DR   EMBL; AE013218; AAM67755.1; -; Genomic_DNA.
DR   RefSeq; NP_660544.1; -.
DR   HSSP; P31663; 1IHO.
DR   GeneID; 1005387; -.
DR   GenomeReviews; AE013218_GR; BUsg_190.
DR   KEGG; bas:BUsg190; -.
DR   HOGENOM; Q8K9U7; -.
DR   OMA; Q8K9U7; MISAENT.
DR   BioCyc; BAPH198804:BUSG190-MON; -.
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:HAMAP.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00158; -; 1.
DR   InterPro; IPR003721; Pantoate_ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR21299:SF1; Pantoate_ligase; 1.
DR   Pfam; PF02569; Pantoate_ligase; 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    285       Pantothenate synthetase.
FT                                /FTId=PRO_0000128213.
FT   NP_BIND      30     37       ATP (By similarity).
FT   NP_BIND     149    152       ATP (By similarity).
FT   NP_BIND     186    189       ATP (By similarity).
FT   ACT_SITE     37     37       Proton donor (By similarity).
FT   BINDING      61     61       Beta-alanine (By similarity).
FT   BINDING      61     61       Pantoate (By similarity).
FT   BINDING     155    155       Pantoate (By similarity).
FT   BINDING     178    178       ATP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
SQ   SEQUENCE   285 AA;  32965 MW;  28DEE9F09FE84B53 CRC64;
     MNIIKNINLL EKKIKELKKK NKIIGLVPTM GNLHDGHIKL ILLAKKNVDI VIVSIFINPM
     QFEDLLDLKK YPKTFEQDCC ILKQEKVEIL FCPDVNEMYP LGLKNHTYID VPKLSKIIEG
     KVRPGHFIGV TTIVCKLFNL IQPNFSFFGE KDYQQLLIIK KLVKELNYPI KIISLPIIRL
     KNGLAFSSRN KHLSDLAQQK ASYLYQAIKQ TCNFIKNNNG KNIKKNIHTS RKYLIKKGFY
     IDIFNAYDSK TLDPISKDSK NIIIIASVWL GKIRLIDNKK IILRD
//