ID   PANC_BARHE              Reviewed;         284 AA.
AC   Q6G456;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   16-JUN-2009, entry version 30.
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=BH05120;
OS   Bartonella henselae (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=38323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(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; BX897699; CAF27320.1; ALT_INIT; Genomic_DNA.
DR   GenomeReviews; BX897699_GR; BH05120.
DR   KEGG; bhe:BH05120; -.
DR   NMPDR; fig|283166.1.peg.476; -.
DR   HOGENOM; Q6G456; -.
DR   BioCyc; BHEN283166:BH05120-MON; -.
DR   BRENDA; 6.3.2.1; 277357.
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    284       Pantothenate synthetase.
FT                                /FTId=PRO_0000128206.
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   284 AA;  32021 MW;  12914B6A1302A413 CRC64;
     MRVLKTIPEV RQSITEERRL GFSIGLVPTM GALHNGHIAL VRRARAMCDR VLVSIFVNPK
     QFGPDEDFDK YPRDLKGDCA LLEEAGVEYL FTPSVEEMWP PGNETIVNVE KLSRMLIGKL
     RPGHFCGVTS VVAKLFNIVQ PDKAFFGEKD FQQILIVRRM VEDLAFPIEV VGVPVLREAD
     GVASSSRNQF LTLEDRKAAK IIPESGKAAE NLYRQGERSV DKLCKIVRDI LQQESRAIIE
     SIDLRDMETL SVVKGRLDKS AVLLLTVRFG EIRLIDQYIL QEKG
//