ID   PANC2_FRAAA             Reviewed;         330 AA.
AC   Q0REL2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Pantothenate synthetase 2;
DE            Short=PS 2;
DE            EC=6.3.2.1;
DE   AltName: Full=Pantoate--beta-alanine ligase 2;
DE   AltName: Full=Pantoate-activating enzyme 2;
GN   Name=panC2; OrderedLocusNames=FRAAL5463;
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; CAJ64096.1; -; Genomic_DNA.
DR   RefSeq; YP_715623.1; -.
DR   GeneID; 4234010; -.
DR   GenomeReviews; CT573213_GR; FRAAL5463.
DR   KEGG; fal:FRAAL5463; -.
DR   BioCyc; FALN326424:FRAAL5463-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.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis.
FT   CHAIN         1    330       Pantothenate synthetase 2.
FT                                /FTId=PRO_0000305454.
FT   NP_BIND     167    170       ATP (By similarity).
FT   NP_BIND     204    207       ATP (By similarity).
FT   ACT_SITE     55     55       Proton donor (By similarity).
FT   BINDING     196    196       ATP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
SQ   SEQUENCE   330 AA;  34091 MW;  0782103C69ED6697 CRC64;
     MSGNGGGIGT GLGSLAGSGR TVTTIAEVRA AADAVRAAGG RVGFFGTSGA LHEGHLTVIR
     RMAAECDLSI MPLFLAPVPG VTSDAVPAYD RDFDADAALA FDAGVNLVFR PAVAEMYPAL
     PVRTAVVPAD ELAAPWEGAE DPSFLRMAAT ALAKYYNIVG PCRAYTGEKD WVPLTVLRRM
     VVDLSIRAEI VACPVVRLAD GLCASSRNSR LSAADRAAAP TLYAALTAAV AAVEAGERDA
     EAIRSLLRRR ISAVAPVDYA EVVDATTLAR VDPLAGELRL LVSADFTGTH LFDNVGLTVR
     DADADADARV TVPAVGTTAA APATDRRTSG
//