ID PANC_GEOMG Reviewed; 283 AA.
AC Q39V50;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 01-MAY-2013, entry version 50.
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=Gmet_1643;
OS Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS-15 / ATCC 53774 / DSM 7210;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; (R)-pantothenate biosynthesis;
CC (R)-pantothenate from (R)-pantoate and beta-alanine: 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; CP000148; ABB31874.1; -; Genomic_DNA.
DR RefSeq; YP_006720610.1; NC_007517.1.
DR HSSP; P0A5R0; 2A84.
DR ProteinModelPortal; Q39V50; -.
DR SMR; Q39V50; 1-280.
DR STRING; 269799.Gmet_1643; -.
DR EnsemblBacteria; ABB31874; ABB31874; Gmet_1643.
DR GeneID; 3740412; -.
DR KEGG; gme:Gmet_1643; -.
DR PATRIC; 22002512; VBIGeoMet55070_1682.
DR eggNOG; COG0414; -.
DR HOGENOM; HOG000175516; -.
DR KO; K01918; -.
DR OMA; HTIVSVF; -.
DR ProtClustDB; PRK00380; -.
DR BioCyc; GMET269799:GHNY-1666-MONOMER; -.
DR UniPathway; UPA00028; UER00005.
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 Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00158; PanC; 1; -.
DR InterPro; IPR003721; Pantoate_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21299:SF1; PTHR21299:SF1; 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 1 283 Pantothenate synthetase.
FT /FTId=PRO_0000305458.
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 283 AA; 31106 MW; F1AE4C485F051289 CRC64;
MRIIETVAEM QAFSREARRE GKSISLVPTM GFLHEGHASL MIEGKKRADI LVTSIFVNPT
QFGPTEDFDA YPRDLARDRN VAETAGVDVI FAPKASDMYP RGFQTYVNVE ELTRPLCGAS
RPGHFQGVTT VVAKLLNIVL PHVALFGKKD FQQLAVIRRM AADLNMDVEI VGMPIVREAD
GLAMSSRNAY LGPEERKNAL CLSRALATAR DLFLDGERSV GTLRDKVLRV IGEVPGAVID
YADFRDGDTL ETVETANGRT LIALAVKIGK TRLIDNCILG EEQ
//
