ID   PANC_LOTJA              Reviewed;         308 AA.
AC   O24035;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   13-SEP-2023, entry version 110.
DE   RecName: Full=Pantoate--beta-alanine ligase;
DE            EC=6.3.2.1;
DE   AltName: Full=Pantoate-activating enzyme;
DE   AltName: Full=Pantothenate synthetase;
DE   Flags: Precursor;
GN   Name=PANC;
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-17, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Gifu / B-129; TISSUE=Root nodule;
RX   PubMed=10417331; DOI=10.1042/0264-6021:3410669;
RA   Genschel U., Powell C.A., Abell C., Smith A.G.;
RT   "The final step of pantothenate biosynthesis in higher plants: cloning and
RT   characterization of pantothenate synthetase from Lotus japonicus and Oryza
RT   sativum (rice).";
RL   Biochem. J. 341:669-678(1999).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.8. Activity decreases sharply with increasing acidity
CC         and is null at pH 7. There is only a slight decrease toward higher
CC         pH.;
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in leaf and root.
CC       {ECO:0000269|PubMed:10417331}.
CC   -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; Y10252; CAA71302.1; -; mRNA.
DR   AlphaFoldDB; O24035; -.
DR   SMR; O24035; -.
DR   OMA; CNHKLEP; -.
DR   BioCyc; MetaCyc:MONOMER-9445; -.
DR   BRENDA; 6.3.2.1; 3076.
DR   UniPathway; UPA00028; UER00005.
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-EC.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00560; PanC; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.30.1300.10; Pantoate-beta-alanine ligase, C-terminal domain; 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   NCBIfam; TIGR00018; panC; 1.
DR   PANTHER; PTHR21299; CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE; 1.
DR   PANTHER; PTHR21299:SF1; PANTOATE--BETA-ALANINE LIGASE; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Ligase;
KW   Nucleotide-binding; Pantothenate biosynthesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10417331"
FT   PROPEP          2
FT                   /note="Removed; partial"
FT                   /id="PRO_0000023005"
FT   CHAIN           3..308
FT                   /note="Pantoate--beta-alanine ligase"
FT                   /id="PRO_0000023006"
SQ   SEQUENCE   308 AA;  34240 MW;  13344F2A8508D2D0 CRC64;
     MAPMVISDKD EMRKWSRSMR SQGKLIALVP TMGFLHEGHL SLVRDAHNHA DLVAVSIYVN
     PGQFSPTEDL SAYPSDFQGD LQKLMSVPGG VDVVFHPHNL YDYGGDGGDA VAECGGDGVV
     SCVDRRSGFG HETWVRAEKL EKPLCGKSRP VFFRGVATIV TKLFNIVEPD VAVFGKKDYQ
     QWKIIQRMVR DLDFSIKVIG SEVIREKDGL AMSSRNVYLS PEEREKAVSI NKSLFRAKSA
     AEDGQIHCEK LINLVVQSIT EAGGRIDYAE IVDQNNLEKV EWIKGPVVFC VSAWFGKARL
     IDNIEINL
//