ID   PANC4_FRAAA             Reviewed;         302 AA.
AC   Q0RB94;
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 4;
DE            Short=PS 4;
DE            EC=6.3.2.1;
DE   AltName: Full=Pantoate--beta-alanine ligase 4;
DE   AltName: Full=Pantoate-activating enzyme 4;
GN   Name=panC4; OrderedLocusNames=FRAAL6670;
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; CAJ65293.1; -; Genomic_DNA.
DR   RefSeq; YP_716797.1; -.
DR   GeneID; 4233712; -.
DR   GenomeReviews; CT573213_GR; FRAAL6670.
DR   KEGG; fal:FRAAL6670; -.
DR   OMA; Q0RB94; GGEPQVR.
DR   BioCyc; FALN326424:FRAAL6670-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    302       Pantothenate synthetase 4.
FT                                /FTId=PRO_0000305456.
FT   NP_BIND      51     58       ATP (By similarity).
FT   NP_BIND     166    169       ATP (By similarity).
FT   NP_BIND     203    206       ATP (By similarity).
FT   ACT_SITE     58     58       Proton donor (By similarity).
FT   BINDING      82     82       Beta-alanine (By similarity).
FT   BINDING      82     82       Pantoate (By similarity).
FT   BINDING     172    172       Pantoate (By similarity).
FT   BINDING     195    195       ATP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
SQ   SEQUENCE   302 AA;  31350 MW;  CD83BD88735FEE29 CRC64;
     MLVRDRAELR AALVALDRAA SSHPPAAAQD AGPARAASRH DRPVRAVVMT MGALHEGHAS
     LLRAARARAD QVVATIFVNP LQFGAGEDLD RYPRTLAADL AVCAREGVDV VFAPAVIHDP
     PPLVRFGAGP LGAVLEGASR PGHFDGMLTL VGTMLHLVQP DLAFFGRKDA QQLVCIRRMV
     ADLAFDVTVI GVETAREPDG LARSSRNVYL TAEQRTEALA LSRALAAGAA ASADGAPAVL
     AAARAVLDAA DGVDVDYLEL AGPEDLGPVR GGPALLLVAA RVGTTRLIDN VSLILPTDTQ
     GA
//