PANC_YERPE
ID PANC_YERPE Reviewed; 284 AA.
AC Q8ZBK7; Q0WBP4;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
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};
GN OrderedLocusNames=YPO3402, y0785, YP_0283;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(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; AL590842; CAL21991.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84372.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS60558.1; -; Genomic_DNA.
DR PIR; AD0413; AD0413.
DR RefSeq; WP_002209348.1; NZ_WUCM01000008.1.
DR RefSeq; YP_002348294.1; NC_003143.1.
DR PDB; 3Q10; X-ray; 1.83 A; A/B/C/D=1-284.
DR PDB; 3Q12; X-ray; 1.58 A; A/B/C/D=1-284.
DR PDBsum; 3Q10; -.
DR PDBsum; 3Q12; -.
DR AlphaFoldDB; Q8ZBK7; -.
DR SMR; Q8ZBK7; -.
DR STRING; 214092.YPO3402; -.
DR PaxDb; Q8ZBK7; -.
DR DNASU; 1145732; -.
DR EnsemblBacteria; AAM84372; AAM84372; y0785.
DR EnsemblBacteria; AAS60558; AAS60558; YP_0283.
DR GeneID; 57975307; -.
DR KEGG; ype:YPO3402; -.
DR KEGG; ypk:y0785; -.
DR KEGG; ypm:YP_0283; -.
DR PATRIC; fig|214092.21.peg.3887; -.
DR eggNOG; COG0414; Bacteria.
DR HOGENOM; CLU_047148_0_0_6; -.
DR OMA; CNHKLEP; -.
DR UniPathway; UPA00028; UER00005.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IBA:GO_Central.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IBA:GO_Central.
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; 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; TIGR00018; panC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Pantothenate biosynthesis; Reference proteome.
FT CHAIN 1..284
FT /note="Pantothenate synthetase"
FT /id="PRO_0000128295"
FT ACT_SITE 37
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 61
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 61
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 149..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 155
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 186..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:3Q12"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:3Q12"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3Q12"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:3Q12"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:3Q12"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3Q12"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:3Q12"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:3Q12"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3Q12"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:3Q12"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3Q12"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3Q12"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3Q12"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3Q12"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:3Q12"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:3Q12"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:3Q12"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:3Q12"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:3Q12"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:3Q12"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:3Q12"
FT HELIX 222..236
FT /evidence="ECO:0007829|PDB:3Q12"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:3Q12"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3Q12"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:3Q12"
FT STRAND 272..281
FT /evidence="ECO:0007829|PDB:3Q12"
SQ SEQUENCE 284 AA; 31772 MW; 6F589341B134FA7F CRC64;
MLIIETLPLL RQQIRRWRQE GKRIALVPTM GNLHEGHMTL VDEAKTRADV VVVTIFVNPL
QFERPDDLAH YPRTLQEDCE KLTRHGADLV FAPAAADIYP AGLEKQTYVD VPALSTILEG
ASRPGHFRGV STIVSKLFNL IQPDVACFGE KDYQQLALIR KMVADMGYDI NIVGVPTVRA
KDGLALSSRN GYLTEEERQI APQLSKIMWA LAEKMALGER QIDALLEEAA AQLLRVGFTP
DELFIRDAET LQPLTVDSQQ AVILMAAWLG KARLIDNQLV DLRH
