ID   PANC_ALCBS              Reviewed;         285 AA.
AC   Q0VSR4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=ABO_0336;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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; AM286690; CAL15784.1; -; Genomic_DNA.
DR   RefSeq; YP_692056.1; -.
DR   GeneID; 4212436; -.
DR   GenomeReviews; AM286690_GR; ABO_0336.
DR   KEGG; abo:ABO_0336; -.
DR   NMPDR; fig|393595.12.peg.336; -.
DR   HOGENOM; Q0VSR4; -.
DR   OMA; Q0VSR4; FGSYPRT.
DR   BioCyc; ABOR393595:ABO_0336-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; 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    285       Pantothenate synthetase.
FT                                /FTId=PRO_0000305388.
FT   NP_BIND      30     37       ATP (By similarity).
FT   NP_BIND     148    151       ATP (By similarity).
FT   NP_BIND     185    188       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     154    154       Pantoate (By similarity).
SQ   SEQUENCE   285 AA;  31267 MW;  21F2417614FDA8E5 CRC64;
     MQTAHSVAQV REHVRGWHRK GQSVGFVPTM GNLHDGHISL VREARTRCDV VVVSIFVNPT
     QFGPNEDFDR YPRTLDADAA ALVEAGADLL FAPSVEEMYP LGQNQTWVDV DQLGDHLCGA
     SREGHFRGVT TVVSKLLNIV QPDVAIFGEK DFQQLAILRR MCEELLFPVK IVGAATSRET
     DGLARSSRNG FLSESERTLA PQLYAHLQQV KTEIIGGERN YRALESRTSQ SLNSTGFSVD
     YITIANARTL APAGPDDTDL IVAVAAKLGS TRLIDNISLA VVRDR
//