PANC_BRUME
ID PANC_BRUME Reviewed; 293 AA.
AC Q8YFC9;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=BMEI1593;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE008917; AAL52774.1; -; Genomic_DNA.
DR PIR; AC3451; AC3451.
DR RefSeq; WP_004682909.1; NZ_GG703778.1.
DR PDB; 3INN; X-ray; 2.10 A; A/B/C/D=1-293.
DR PDBsum; 3INN; -.
DR AlphaFoldDB; Q8YFC9; -.
DR SMR; Q8YFC9; -.
DR STRING; 224914.BMEI1593; -.
DR EnsemblBacteria; AAL52774; AAL52774; BMEI1593.
DR GeneID; 45123829; -.
DR KEGG; bme:BMEI1593; -.
DR PATRIC; fig|224914.52.peg.1997; -.
DR eggNOG; COG0414; Bacteria.
DR OMA; CNHKLEP; -.
DR PhylomeDB; Q8YFC9; -.
DR UniPathway; UPA00028; UER00005.
DR EvolutionaryTrace; Q8YFC9; -.
DR Proteomes; UP000000419; Chromosome I.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Pantothenate biosynthesis.
FT CHAIN 1..293
FT /note="Pantothenate synthetase"
FT /id="PRO_0000128210"
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 147..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 153
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 184..187
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:3INN"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:3INN"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3INN"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:3INN"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:3INN"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3INN"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3INN"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:3INN"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3INN"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:3INN"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:3INN"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:3INN"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:3INN"
FT HELIX 124..139
FT /evidence="ECO:0007829|PDB:3INN"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3INN"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:3INN"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:3INN"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:3INN"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:3INN"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:3INN"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:3INN"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:3INN"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:3INN"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:3INN"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:3INN"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:3INN"
SQ SEQUENCE 293 AA; 32524 MW; BF9F2C983D14E2D1 CRC64;
MQIIHTIEEL RQALAPARQQ GKKIGFVPTM GYLHKGHLEL VRRARVENDV TLVSIFVNPL
QFGANEDLGR YPRDLERDAG LLHDAQVDYL FAPTVSDMYP RPMQTVVDVP PLGNQMEGEA
RPGHFAGVAT VVSKLFNIVG PDAAYFGEKD FQQLVIIRRM VDDMAIPVRI VGVETVREDD
GLACSSRNVY LTPEQRRAAI IVPQALDEAD RLYRSGMDDP DALEAAIRTF IGRQPLAVPE
VIAIRDPETL ERLPALQGRP ILVALFVRVG ATRLLDNRVI GHAAPQITQE RAA
