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143  structures 6390  species 0  interactions 7327  sequences 36  architectures

Family: Pantoate_ligase (PF02569)

Summary: Pantoate-beta-alanine ligase

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Pantoate—beta-alanine ligase". More...

Pantoate—beta-alanine ligase Edit Wikipedia article

pantoate-beta-alanine ligase
EC number6.3.2.1
CAS number9023-49-8
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a pantoate-beta-alanine ligase (EC is an enzyme that catalyzes the chemical reaction

ATP + (R)-pantoate + beta-alanine AMP + diphosphate + (R)-pantothenate

The 3 substrates of this enzyme are ATP, (R)-pantoate, and beta-alanine, whereas its 3 products are AMP, diphosphate, and (R)-pantothenate.

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is (R)-pantoate:beta-alanine ligase (AMP-forming). Other names in common use include pantothenate synthetase, pantoate activating enzyme, pantoic-activating enzyme, and D-pantoate:beta-alanine ligase (AMP-forming). This enzyme participates in beta-alanine metabolism and pantothenate and CoA biosynthesis.

Structural studies

As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes 1IHO, 1MOP, 1N2B, 1N2E, 1N2G, 1N2H, 1N2I, 1N2J, 1N2O, 1UFV, 1V8F, 2A7X, 2A84, 2A86, and 2A88.


  • GINOZA HS, ALTENBERN RA (1955). "The pantothenate-synthesizing enzyme in cell-free extracts of Brucella abortus, strain 19". Arch. Biochem. 56 (2): 537–41. doi:10.1016/0003-9861(55)90273-3. PMID 14377603.
  • MAAS WK (1952). "Pantothenate studies. III. Description of the extracted pantothenate-synthesizing enzyme of Escherichia coli". J. Biol. Chem. 198 (1): 23–32. PMID 12999714.
  • Maas WK (1956). "Mechanism of the enzymatic synthesis of pantothenate from beta-alanine and pantoate". Fed. Proc. 15: 305–306.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Pantoate-beta-alanine ligase Provide feedback

Pantoate-beta-alanine ligase, also know as pantothenate synthase, ( EC: catalyses the formation of pantothenate from pantoate and alanine [1].

Literature references

  1. Miyatake K, Nakano Y, Kitaoka S; , Methods Enzymol 1979;62:215-219.: Pantothenate synthetase from Escherichia coli [D-pantoate: beta-alanine ligase (AMP-forming), EC]. PUBMED:374975 EPMC:374975

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003721

D-Pantothenate is synthesized via four enzymes from ketoisovalerate, which is an intermediate of branched-chain amino acid synthesis [ PUBMED:10223988 ]. Pantoate-beta-alanine ligase, also know as pantothenate synthase, (PanC; EC ) catalyzes the formation of pantothenate from pantoate and alanine in the pantothenate biosynthesis pathway [ PUBMED:8760912 ].

PanC belongs to a large superfamily of nucleotidyltransferases that includes ATP sulfurylase (ATPS), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain [ PUBMED:15565250 , PUBMED:7479698 , PUBMED:374975 , PUBMED:7037743 , PUBMED:10417331 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan HUP (CL0039), which has the following description:

The HUP class contains the HIGH-signature proteins, UspA superfamily and the PP-ATPase superfamily [1]. The HIGH superfamily has the HIGH Nucleotidyl transferases and the class I tRNA synthetases both of which have the HIGH and the KMSKS motif [1],[2]. The PP-loop ATPase named after the ATP PyroPhosphatase domain, was initially identified as a conserved amino acid sequence motif in four distinct groups of enzymes that catalyse the hydrolysis of the alpha-beta phosphate bond of ATP, namely GMP synthetases, argininosuccinate synthetases, asparagine synthetases, and ATP sulfurylases [3]. The USPA superfamily contains USPA, ETFP and Photolyases [1]

The clan contains the following 31 members:

Arginosuc_synth Asn_synthase ATP-sulfurylase ATP_bind_3 BshC CDPS Citrate_ly_lig CTP_transf_like Diphthami_syn_2 DNA_photolyase DPRP ETF FAD_syn HIGH_NTase1 HIGH_NTase1_ass NAD_synthase Pantoate_ligase PAPS_reduct QueC ThiI tRNA-synt_1 tRNA-synt_1_2 tRNA-synt_1b tRNA-synt_1c tRNA-synt_1d tRNA-synt_1e tRNA-synt_1f tRNA-synt_1g tRNA_Me_trans UDPG_MGDP_dh_C Usp


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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Curation and family details

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Seed source: COGs
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Mian N , Bateman A
Number in seed: 664
Number in full: 7327
Average length of the domain: 276.60 aa
Average identity of full alignment: 40 %
Average coverage of the sequence by the domain: 92.78 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 20.8 20.7
Noise cut-off 20.6 20.6
Model length: 265
Family (HMM) version: 17
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Species distribution

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Archea Archea Eukaryota Eukaryota
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Pantoate_ligase domain has been found. There are 143 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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