PANC1_BRADU
ID PANC1_BRADU Reviewed; 283 AA.
AC Q9AMR9;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Pantothenate synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00158};
DE Short=PS 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00158};
DE AltName: Full=Pantoate-activating enzyme 1 {ECO:0000255|HAMAP-Rule:MF_00158};
GN Name=panC1 {ECO:0000255|HAMAP-Rule:MF_00158}; OrderedLocusNames=blr2102;
GN ORFNames=id912;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RX PubMed=11157954; DOI=10.1128/jb.183.4.1405-1412.2001;
RA Goettfert M., Roethlisberger S., Kuendig C., Beck C., Marty R.,
RA Hennecke H.;
RT "Potential symbiosis-specific genes uncovered by sequencing a 410-kb DNA
RT region of the Bradyrhizobium japonicum chromosome.";
RL J. Bacteriol. 183:1405-1412(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(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}.
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DR EMBL; AF322013; AAG61078.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC47367.1; -; Genomic_DNA.
DR RefSeq; NP_768742.1; NC_004463.1.
DR RefSeq; WP_011084897.1; NZ_CP011360.1.
DR AlphaFoldDB; Q9AMR9; -.
DR SMR; Q9AMR9; -.
DR STRING; 224911.27350356; -.
DR EnsemblBacteria; BAC47367; BAC47367; BAC47367.
DR GeneID; 64021856; -.
DR KEGG; bja:blr2102; -.
DR PATRIC; fig|224911.44.peg.1612; -.
DR eggNOG; COG0414; Bacteria.
DR HOGENOM; CLU_047148_0_0_5; -.
DR InParanoid; Q9AMR9; -.
DR OMA; CNHKLEP; -.
DR PhylomeDB; Q9AMR9; -.
DR UniPathway; UPA00028; UER00005.
DR Proteomes; UP000002526; 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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Pantothenate biosynthesis; Reference proteome.
FT CHAIN 1..283
FT /note="Pantothenate synthetase 1"
FT /id="PRO_0000128208"
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"
SQ SEQUENCE 283 AA; 31322 MW; A2CA526734D9A607 CRC64;
MKVITKVAEL RRALADVRNA EKRIGFVPTM GYLHDGHLAL ISASREHCDV TVVSIFVNPT
QFGPNEDLSR YPRDFARDEA LCGSAGVSII FAPSAEEIYP AQFESFVEPG ELAKPLCGAF
RPGHFRGVAT VVCKLFNMVQ PDVAYFGQKD FQQCAVIRRM TVDLNLPIEI VTVPTVREPD
GLAMSSRNRY LCPEERDRSL AISRGLFAAA HEFASGERDA ATLIALARRH LERVDRLQYL
ELVDPGTLRI ADSPLRYPAV LCVAAYVGST RLIDNVVLSW SPS
