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C0ZCH1 (C0ZCH1_BREBN) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pantothenate synthetase HAMAP MF_00158
Short name=PS HAMAP MF_00158
EC=6.3.2.1 HAMAP MF_00158
Alternative name(s):
Pantoate--beta-alanine ligase HAMAP MF_00158
Pantoate-activating enzyme HAMAP MF_00158
Gene names
Name:panC HAMAP MF_00158 EMBL BAH43480.1
Ordered Locus Names:BBR47_25030
OrganismBrevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599) [Complete proteome] [HAMAP]
Taxonomic identifier358681 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Paenibacillaceae › Brevibacillus

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity. HAMAP MF_00158

Catalytic activity

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP MF_00158

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP MF_00158

Subunit structure

Homodimer By similarity. HAMAP MF_00158

Subcellular location

Cytoplasm By similarity HAMAP MF_00158.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP MF_00158

Sequence similarities

Belongs to the pantothenate synthetase family. HAMAP MF_00158

Ontologies

Keywords
   Biological processPantothenate biosynthesis HAMAP MF_00158
   Cellular componentCytoplasm HAMAP MF_00158
   LigandATP-binding HAMAP MF_00158
Nucleotide-binding
   Molecular functionLigase HAMAP MF_00158 EMBL BAH43480.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpantothenate biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

pantoate-beta-alanine ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding35 – 428ATP By similarity HAMAP MF_00158
Nucleotide binding152 – 1554ATP By similarity HAMAP MF_00158
Nucleotide binding189 – 1924ATP By similarity HAMAP MF_00158

Sites

Active site421Proton donor By similarity HAMAP MF_00158
Binding site661Beta-alanine By similarity HAMAP MF_00158
Binding site661Pantoate By similarity HAMAP MF_00158
Binding site1581Pantoate By similarity HAMAP MF_00158
Binding site1811ATP; via amide nitrogen and carbonyl oxygen By similarity HAMAP MF_00158

Sequences

Sequence LengthMass (Da)Tools
C0ZCH1 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: ADB7CA8C9803390B

FASTA28831,966
        10         20         30         40         50         60 
MMQTMMQQVS TIAEMRVHLK DARRQGKTIG MVPTMGFLHE GHLSLVKAAR EVCDLVVMSI 

        70         80         90        100        110        120 
FVNPLQFGPN EDFERYPRDI ERDSKMAEEA GVDFLFTPEV SEMYPTPMLT NISVANVTTP 

       130        140        150        160        170        180 
LCGASRPGHF DGVSTVVNKL FQIVQPDYAF FGQKDAQQVA VVTQMVHDLS MPVQIVPCPI 

       190        200        210        220        230        240 
VREADGLALS SRNVYLSADE RTQALVLSQS LRQAEEWLSE GVALSTIKDR ITQMISEKPL 

       250        260        270        280 
ADIDYVEILS YPALTPMAQE TAGQTIIIAL AVRFGKTRLI DNTITSIK

« Hide

References

[1]"Brevibacillus brevis strain 47, complete genome."
Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W., Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S., Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H. expand/collapse author list , Udaka S., Tanikawa S., Fujita N.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP008955 Genomic DNA. Translation: BAH43480.1.
RefSeqYP_002771984.1. NC_012491.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGC0ZCH1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7719841.
GenomeReviewsGene locus BBR47_25030 in contig AP008955_GR.
KEGGbbe:BBR47_25030.
PATRIC21235330. VBIBreBre96763_2488.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMALNMPIQI.
ProtClustDBCLSK2547246.

Family and domain databases

HAMAPMF_00158. PanC.
[Tree]
InterProIPR004821. Cyt_trans-rel.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01918.
PANTHERPTHR21299:SF1. Pantoate_ligase. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. Cyt_tran_rel. 1 hit.
TIGR00018. PanC. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC0ZCH1_BREBN
AccessionPrimary (citable) accession number: C0ZCH1
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: December 14, 2011
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info