ID   PANC_BORA1              Reviewed;         280 AA.
AC   Q2KUK2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=BAV3048;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ50658.1; -; Genomic_DNA.
DR   RefSeq; YP_787543.1; -.
DR   GeneID; 6266352; -.
DR   GenomeReviews; AM167904_GR; BAV3048.
DR   KEGG; bav:BAV3048; -.
DR   NMPDR; fig|521.1.peg.2163; -.
DR   HOGENOM; Q2KUK2; -.
DR   OMA; Q2KUK2; SRNVYLN.
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; IPR004821; Cyt_trans_rel.
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; TIGR00125; cyt_tran_rel; 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    280       Pantothenate synthetase.
FT                                /FTId=PRO_0000305405.
FT   NP_BIND      26     33       ATP (By similarity).
FT   NP_BIND     145    148       ATP (By similarity).
FT   NP_BIND     182    185       ATP (By similarity).
FT   ACT_SITE     33     33       Proton donor (By similarity).
FT   BINDING      57     57       Beta-alanine (By similarity).
FT   BINDING      57     57       Pantoate (By similarity).
FT   BINDING     151    151       Pantoate (By similarity).
FT   BINDING     174    174       ATP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
SQ   SEQUENCE   280 AA;  31856 MW;  4677BCF5CD0C75FC CRC64;
     MKVVHTIQDL RDHLRGQNRI AFVPTMGNLH EGHLALMKLA RQHGDPVVTS IFVNRLQFGP
     NEDFDRYPRT LQNDIEKMDR DRDVYMVFAP DEREMYPEPQ NYRVLPPDDL GDVLEGEFRP
     GFFQGVCTVV LKLLSCVQPR VAVFGKKDYQ QLMIVRAMCR QFQLPVEIIA HETVRASDGL
     ALSSRNRYLS VEERAEAPRL YALLGELRQR VLDGERDVAA LEAEAAARLA AHGWRVDYVS
     LRRQHDLKTP GAADFETRQP LVALAAATLG ATRLIDNLEI
//