PANC_LEIXX
ID PANC_LEIXX Reviewed; 287 AA.
AC Q6ACQ8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Pantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_00158};
DE Short=PS {ECO:0000255|HAMAP-Rule:MF_00158};
DE EC=6.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00158};
DE AltName: Full=Pantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00158};
DE AltName: Full=Pantoate-activating enzyme {ECO:0000255|HAMAP-Rule:MF_00158};
GN Name=panC {ECO:0000255|HAMAP-Rule:MF_00158}; OrderedLocusNames=Lxx21410;
OS Leifsonia xyli subsp. xyli (strain CTCB07).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia.
OX NCBI_TaxID=281090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTCB07;
RX PubMed=15305603; DOI=10.1094/mpmi.2004.17.8.827;
RA Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P.,
RA Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D.,
RA de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R.,
RA Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L.,
RA El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli
RT subsp. xyli.";
RL Mol. Plant Microbe Interact. 17:827-836(2004).
CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in
CC an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC {ECO:0000255|HAMAP-Rule:MF_00158}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP +
CC diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00158};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00158}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00158}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00158}.
CC -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong
CC mechanism. {ECO:0000255|HAMAP-Rule:MF_00158}.
CC -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00158}.
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DR EMBL; AE016822; AAT89835.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6ACQ8; -.
DR SMR; Q6ACQ8; -.
DR STRING; 281090.Lxx21410; -.
DR EnsemblBacteria; AAT89835; AAT89835; Lxx21410.
DR KEGG; lxx:Lxx21410; -.
DR eggNOG; COG0414; Bacteria.
DR HOGENOM; CLU_047148_0_2_11; -.
DR OMA; CNHKLEP; -.
DR UniPathway; UPA00028; UER00005.
DR Proteomes; UP000001306; Chromosome.
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:UniProtKB-UniRule.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00560; PanC; 1.
DR Gene3D; 3.30.1300.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00158; PanC; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR003721; Pantoate_ligase.
DR InterPro; IPR042176; Pantoate_ligase_C.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21299:SF1; PTHR21299:SF1; 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; Cytoplasm; Ligase; Nucleotide-binding;
KW Pantothenate biosynthesis; Reference proteome.
FT CHAIN 1..287
FT /note="Pantothenate synthetase"
FT /id="PRO_0000305471"
FT ACT_SITE 44
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 68
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 68
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 154..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 160
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 191..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
SQ SEQUENCE 287 AA; 30061 MW; 49320EEA1D496D80 CRC64;
MTVIACLREI LSTARRTAVA EGASDAPASR VVLVPTMGAL HEGHVRLVNH ARDLGGIVVV
SIFVNPLQFG PGEDLDRYPR TLDADVALLD GLADVVFAPA AAEMYPQGES STRVTAGAVG
GLFEGASRPG HFDGMLTVVA KLFGIAQPDV AVFGQKDAQQ VHLVGRMVDD LNLPVTIAVV
DTVREPDGLA LSSRNRYLDA DARAAAATLS RALADGVAAC AGGAAAVLTA ARVRVEAEPV
VRLDYLVIVD QGTFREVAPN YHGPAFLLIA ARVGSTRLID NERITLP
