PANC_MYCTO
ID PANC_MYCTO Reviewed; 309 AA.
AC P9WIL4; L0TG74; O06280; P0A5R0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
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=MT3707;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in
CC an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC {ECO:0000250}.
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 -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK48065.1; -; Genomic_DNA.
DR PIR; C70955; C70955.
DR RefSeq; WP_003419526.1; NZ_KK341227.1.
DR PDB; 4MQ6; X-ray; 1.70 A; A/B=3-309.
DR PDB; 4MUE; X-ray; 2.06 A; A/B=3-300.
DR PDB; 4MUF; X-ray; 2.50 A; A/B=3-300.
DR PDB; 4MUG; X-ray; 1.54 A; A/B=3-300.
DR PDB; 4MUH; X-ray; 1.72 A; A/B=3-300.
DR PDB; 4MUI; X-ray; 2.10 A; A/B=3-300.
DR PDB; 4MUJ; X-ray; 1.92 A; A/B=3-300.
DR PDB; 4MUK; X-ray; 1.90 A; A/B=3-300.
DR PDB; 4MUL; X-ray; 1.75 A; A/B=3-300.
DR PDB; 4MUN; X-ray; 1.57 A; A/B=3-300.
DR PDBsum; 4MQ6; -.
DR PDBsum; 4MUE; -.
DR PDBsum; 4MUF; -.
DR PDBsum; 4MUG; -.
DR PDBsum; 4MUH; -.
DR PDBsum; 4MUI; -.
DR PDBsum; 4MUJ; -.
DR PDBsum; 4MUK; -.
DR PDBsum; 4MUL; -.
DR PDBsum; 4MUN; -.
DR AlphaFoldDB; P9WIL4; -.
DR SMR; P9WIL4; -.
DR EnsemblBacteria; AAK48065; AAK48065; MT3707.
DR KEGG; mtc:MT3707; -.
DR PATRIC; fig|83331.31.peg.3990; -.
DR HOGENOM; CLU_047148_0_2_11; -.
DR UniPathway; UPA00028; UER00005.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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; 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; Magnesium; Metal-binding;
KW Nucleotide-binding; Pantothenate biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..309
FT /note="Pantothenate synthetase"
FT /id="PRO_0000427985"
FT ACT_SITE 47
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 158..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 195..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:4MUG"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:4MUG"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4MUG"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:4MUG"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:4MUG"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 135..150
FT /evidence="ECO:0007829|PDB:4MUG"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:4MUG"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 228..240
FT /evidence="ECO:0007829|PDB:4MUG"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:4MUG"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:4MUG"
FT STRAND 264..274
FT /evidence="ECO:0007829|PDB:4MUG"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:4MUG"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:4MQ6"
SQ SEQUENCE 309 AA; 32678 MW; EB51DBE3485F970A CRC64;
MTIPAFHPGE LNVYSAPGDV ADVSRALRLT GRRVMLVPTM GALHEGHLAL VRAAKRVPGS
VVVVSIFVNP MQFGAGEDLD AYPRTPDDDL AQLRAEGVEI AFTPTTAAMY PDGLRTTVQP
GPLAAELEGG PRPTHFAGVL TVVLKLLQIV RPDRVFFGEK DYQQLVLIRQ LVADFNLDVA
VVGVPTVREA DGLAMSSRNR YLDPAQRAAA VALSAALTAA AHAATAGAQA ALDAARAVLD
AAPGVAVDYL ELRDIGLGPM PLNGSGRLLV AARLGTTRLL DNIAIEIGTF AGTDRPDGYR
AILESHWRN
