ID   PANC3_FRAAA             Reviewed;         294 AA.
AC   Q0RC35;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Pantothenate synthetase 3;
DE            Short=PS 3;
DE            EC=6.3.2.1;
DE   AltName: Full=Pantoate--beta-alanine ligase 3;
DE   AltName: Full=Pantoate-activating enzyme 3;
GN   Name=panC3; OrderedLocusNames=FRAAL6371;
OS   Frankia alni (strain ACN14a).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Frankineae; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CT573213; CAJ64994.1; -; Genomic_DNA.
DR   RefSeq; YP_716505.1; -.
DR   GeneID; 4233711; -.
DR   GenomeReviews; CT573213_GR; FRAAL6371.
DR   KEGG; fal:FRAAL6371; -.
DR   OMA; Q0RC35; ASSKENH.
DR   BioCyc; FALN326424:FRAAL6371-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    294       Pantothenate synthetase 3.
FT                                /FTId=PRO_0000305455.
FT   NP_BIND      31     38       ATP (By similarity).
FT   NP_BIND     154    157       ATP (By similarity).
FT   NP_BIND     191    194       ATP (By similarity).
FT   ACT_SITE     38     38       Proton donor (By similarity).
FT   BINDING      62     62       Beta-alanine (By similarity).
FT   BINDING      62     62       Pantoate (By similarity).
FT   BINDING     160    160       Pantoate (By similarity).
SQ   SEQUENCE   294 AA;  32511 MW;  DF3A6AE9A22D1B1E CRC64;
     MLRVLHTIED VREQTREWRA AGSSIGCVMT MGALHEGHLS LVDAARRECD KVVLTLFVNP
     IQFGPSEDFD RYPRTEEADF RALRDRECDA VFAPATETIF PLGERRIDQV RTKVVVRGLT
     DVLCGPRRPG HFDGVTTEVL KMLHIVDCDR TYWGEKDYQQ YAVIRAMVED QGLPVKVVPC
     PTMRDVDGLA LSSRNTYLDS GQRAIAPRLY AALRRGARRI AEQGIDVIGE TTKQIAETLL
     AHGFDLVEYV EVYTGSLGPA VAGTPVEELR VFGAVRLGGA RLLDNAAVAD EVGG
//