ID   PANC_BACFR              Reviewed;         282 AA.
AC   Q64XM3;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=BF1003;
OS   Bacteroides fragilis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA
RT   inversions regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD47753.1; -; Genomic_DNA.
DR   RefSeq; YP_098287.1; -.
DR   GeneID; 3081884; -.
DR   GenomeReviews; AP006841_GR; BF1003.
DR   KEGG; bfr:BF1003; -.
DR   NMPDR; fig|295405.3.peg.1066; -.
DR   HOGENOM; Q64XM3; -.
DR   OMA; Q64XM3; SRNVYLN.
DR   BioCyc; BFRA295405:BF1003-MON; -.
DR   BRENDA; 6.3.2.1; 868.
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    282       Pantothenate synthetase.
FT                                /FTId=PRO_0000305398.
FT   NP_BIND      30     37       ATP (By similarity).
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      61     61       Beta-alanine (By similarity).
FT   BINDING      61     61       Pantoate (By similarity).
FT   BINDING     153    153       Pantoate (By similarity).
FT   BINDING     176    176       ATP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
SQ   SEQUENCE   282 AA;  31559 MW;  07E01A9DBB647E25 CRC64;
     MKVIHTIKDL QAELSVLKAQ GKKVGLVPTM GALHAGHASL VKRSVNENEV TVVSVFVNPT
     QFNDKNDLVK YPRTLDADCK LLEACGATYA FAPSVEEMYP EPDTRQFSYA PLDTVMEGAF
     RPGHFNGVCQ IVSKLFEAVK PHRAYFGEKD FQQLAIIREM VRQMQFDLEI VGCPIVREED
     GLALSSRNAR LSAEERENAL KISQTLFKSR TFAATHTVSE TLKFVEDAIT AVPGLRLEYF
     EIVDGNTLQK VDNWNQTSYV VGCITVFCGD VRLIDNIKYK ES
//