ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q6G456

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PANC_BARHE
Primary accession number Q6G456
Secondary accession numbers None
Integrated into Swiss-Prot on October 25, 2005
Sequence was last modified on October 2, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 28)
Name and origin of the protein
Protein name Pantothenate synthetase
Synonyms PS
EC 6.3.2.1
Pantoate--beta-alanine ligase
Pantoate-activating enzyme
Gene name
Name: panC
OrderedLocusNames: BH05120
From
Bartonella henselae (Rochalimaea henselae) [TaxID: 38323] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bartonellaceae; Bartonella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49882 / Houston 1;
DOI=10.1073/pnas.0305659101; PubMed=15210978 [NCBI, ExPASy, EBI, Israel, Japan]
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.;
"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae.";
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BX897699; CAF27320.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase Q6G456.
Enzyme and pathway databases
BioCyc BHEN283166:BH05120-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004592; Molecular function: pantoate-beta-alanine ligase activity (inferred from electronic annotation from HAMAP).
GO:0015940; Biological process: pantothenate biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00158; -; 1.
PBIL [Tree]
InterPro IPR004821; Cyt_trans_rel.
IPR003721; Pantoate_ligase.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
PANTHER PTHR21299:SF1; Pantoate_ligase; 1.
Pfam PF02569; Pantoate_ligase; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00125; cyt_tran_rel; 1.
TIGR00018; panC; 1.
BLOCKS Q6G456.
ProtoNet Q6G456.
Genome annotation databases
GenomeReviews BX897699_GR; BH05120.
KEGG bhe:BH05120; -.
NMPDR fig|283166.1.peg.476; -.
Phylogenomic databases
HOGENOM Q6G456; -.
Genome annotation databases
CMR Q6G456; BH05120.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Pantothenate biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   284  284     Pantothenate synthetase. PRO_0000128206
NP_BIND   30    37  8     ATP (By similarity). 
NP_BIND   147   150  4     ATP (By similarity). 
NP_BIND   184   187  4     ATP (By similarity). 
ACT_SITE   37    37        Proton donor (By similarity). 
BINDING   61    61        Beta-alanine (By similarity). 
BINDING   61    61        Pantoate (By similarity). 
BINDING   153   153        Pantoate (By similarity). 
BINDING   176   176        ATP; via amide nitrogen and carbonyl oxygen (By similarity). 
Sequence information
Length: 284 AA [This is the length of the unprocessed precursor] Molecular weight: 32021 Da [This is the MW of the unprocessed precursor] CRC64: 12914B6A1302A413 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRVLKTIPEV RQSITEERRL GFSIGLVPTM GALHNGHIAL VRRARAMCDR VLVSIFVNPK 

        70         80         90        100        110        120 
QFGPDEDFDK YPRDLKGDCA LLEEAGVEYL FTPSVEEMWP PGNETIVNVE KLSRMLIGKL 

       130        140        150        160        170        180 
RPGHFCGVTS VVAKLFNIVQ PDKAFFGEKD FQQILIVRRM VEDLAFPIEV VGVPVLREAD 

       190        200        210        220        230        240 
GVASSSRNQF LTLEDRKAAK IIPESGKAAE NLYRQGERSV DKLCKIVRDI LQQESRAIIE 

       250        260        270        280 
SIDLRDMETL SVVKGRLDKS AVLLLTVRFG EIRLIDQYIL QEKG
Q6G456 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!