ID   PANC_AZOSE              Reviewed;         276 AA.
AC   Q5NXQ2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, 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=AZOSEA40370; ORFNames=ebA7120;
OS   Azoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CR555306; CAI10162.1; -; Genomic_DNA.
DR   RefSeq; YP_161063.1; -.
DR   GeneID; 3181680; -.
DR   GenomeReviews; CR555306_GR; AZOSEA40370.
DR   KEGG; eba:ebA7120; -.
DR   NMPDR; fig|76114.4.peg.4053; -.
DR   HOGENOM; Q5NXQ2; -.
DR   OMA; Q5NXQ2; SRNVYLN.
DR   BioCyc; ASP76114:EBA7120-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    276       Pantothenate synthetase.
FT                                /FTId=PRO_0000305395.
FT   NP_BIND      27     34       ATP (By similarity).
FT   NP_BIND     145    148       ATP (By similarity).
FT   NP_BIND     182    185       ATP (By similarity).
FT   ACT_SITE     34     34       Proton donor (By similarity).
FT   BINDING      58     58       Beta-alanine (By similarity).
FT   BINDING      58     58       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   276 AA;  30487 MW;  C522DD0EE70341F3 CRC64;
     MQIHTTIQSL RAARAAVSGK VALVPTMGNL HDGHIALMRQ ATGHADSIVA SIFVNRLQFG
     PRDDFDRYPR TFKADCERLE AAGVAHVFAP DEGEMYPQPQ QYHVDPAPAH VTILEGEFRP
     DHFRGVATVV LKLLNIVRPD VALFGKKDYQ QLMVLTNMVR ELAVAVEVVP GETIRATDGL
     ALSSRNGYLS AEERVEAPRL YRELARVRDA VRDGDRDFLK LETEAVAGLA AHGWHPDYIA
     VRRRADLQPP GDANDPLVVL AAAKLGHTRL IDNLEI
//