ID   PANC_BAUCH              Reviewed;         285 AA.
AC   Q1LTN0;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
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=BCI_0231;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF14074.1; -; Genomic_DNA.
DR   RefSeq; YP_588684.1; -.
DR   GeneID; 4056175; -.
DR   GenomeReviews; CP000238_GR; BCI_0231.
DR   KEGG; bci:BCI_0231; -.
DR   HOGENOM; Q1LTN0; -.
DR   OMA; Q1LTN0; VADFNIP.
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_0000305403.
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;  32539 MW;  E3D1F484A338E507 CRC64;
     MLIIDNITIL RQTIKQWRKS IQSIALIPTM GNLHDGHMTI VNQGRSHTNI VIVSIFVNPM
     QFDREEDLFL YPRTLQSDYE KLHKIGVDAV FVPSVETMYR DNINCHTFLD VPNLSSILEG
     IYRPNHFRGV ATIISKLFNL VQPNVVYFGE KDFQQLVLIR QMVRDMNYDI EIIAVPTVRA
     NDGLALSSRN SYLTPEQRKI APKLYQVMQT LVTNLCSGEK NIDVLLNKAA KQLSKFGFTP
     EILEIRDAIT LQPITINSKK VVVLFSAWLG KARLIDNTQV SIPKE
//