ID   PANC1_FRAAA             Reviewed;         291 AA.
AC   Q0RK33;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=Pantothenate synthetase 1;
DE            Short=PS 1;
DE            EC=6.3.2.1;
DE   AltName: Full=Pantoate--beta-alanine ligase 1;
DE   AltName: Full=Pantoate-activating enzyme 1;
GN   Name=panC1; OrderedLocusNames=FRAAL3483;
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; CAJ62127.1; -; Genomic_DNA.
DR   RefSeq; YP_713690.1; -.
DR   GeneID; 4233397; -.
DR   GenomeReviews; CT573213_GR; FRAAL3483.
DR   KEGG; fal:FRAAL3483; -.
DR   OMA; Q0RK33; SVPTVRM.
DR   BioCyc; FALN326424:FRAAL3483-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    291       Pantothenate synthetase 1.
FT                                /FTId=PRO_0000305453.
FT   NP_BIND     147    150       ATP (By similarity).
FT   NP_BIND     184    187       ATP (By similarity).
FT   ACT_SITE     37     37       Proton donor (By similarity).
FT   BINDING     153    153       Pantoate (By similarity).
SQ   SEQUENCE   291 AA;  31255 MW;  13F80CE30982D894 CRC64;
     MITTEKHAEV RELLDAERAA GRRVAMVGTS GGTHAGHISL VEQAKKECDV VAVFWNGALK
     LEWASGGVQA YNRDLAHDQA LFEAAGVDIF YIPMRDDLYQ RPSNTFMAMP GMLRHLTGMP
     EGEHMELLVT MVATLLNIAG PCLTFFGEKD WQQLVMFQRM AEDLHLPSRV IGCPTRREPD
     GVAISSRNTK LSPEQRAAAP ALYAALTAAA DAIAAGERDA RAAAEVALAR LRPVADPDYI
     VAVEAATLRP LDTLDPAAEG GPSDGEVRLL ASVRFGTTPL VDNIGVTVPT A
//