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Q6LMJ5

- PANC_PHOPR

UniProt

Q6LMJ5 - PANC_PHOPR

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Protein

Pantothenate synthetase

Gene
panC, PBPRA3176
Organism
Photobacterium profundum (Photobacterium sp. (strain SS9))
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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

Catalytic activityi

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei37 – 371Proton donor By similarity
Binding sitei61 – 611Beta-alanine By similarity
Binding sitei61 – 611Pantoate By similarity
Binding sitei155 – 1551Pantoate By similarity
Binding sitei178 – 1781ATP; via amide nitrogen and carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 378ATP By similarity
Nucleotide bindingi149 – 1524ATP By similarity
Nucleotide bindingi186 – 1894ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. pantoate-beta-alanine ligase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. pantothenate biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciPPRO298386-WGS:GSSB-3170-MONOMER.
UniPathwayiUPA00028; UER00005.

Names & Taxonomyi

Protein namesi
Recommended name:
Pantothenate synthetase (EC:6.3.2.1)
Short name:
PS
Alternative name(s):
Pantoate--beta-alanine ligase
Pantoate-activating enzyme
Gene namesi
Name:panC
Ordered Locus Names:PBPRA3176
OrganismiPhotobacterium profundum (Photobacterium sp. (strain SS9))
Taxonomic identifieri74109 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium
ProteomesiUP000000593: Chromosome 1

Subcellular locationi

Cytoplasm Reviewed prediction UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Pantothenate synthetaseUniRule annotationPRO_0000128252Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi298386.PBPRA3176.

Structurei

3D structure databases

ProteinModelPortaliQ6LMJ5.
SMRiQ6LMJ5. Positions 1-282.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175516.
KOiK01918.
OMAiHAGHMEL.
OrthoDBiEOG6Z6FZ4.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC.
InterProiIPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6LMJ5-1 [UniParc]FASTAAdd to Basket

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MQTFAEIALL REQIRAWRRE GRRIAFVPTM GNLHDGHLTL VRKAREHADI    50
VVVSIFVNPM QFEKADDLTN YPRTLENDLA KLNSEGVDLV FTPTPEVMYP 100
QGLERQTFVE VPGLSQMLEG ALRPGHFRGV ATVVTKLFNM VQPDVACFGE 150
KDYQQLALLR QMTLDMAMDI EIIGVPTVRE MDGLAMSSRN GYLTVDERQR 200
APVLARTMRW VSSQMRGGRT DYSEIIVDAN DQLRAAGLQP DESYIRDAVT 250
LQAVSEETQQ AVILMSAQLG KARLIDNQVV ELTQPAAPVA EAAES 295
Length:295
Mass (Da):32,986
Last modified:July 5, 2004 - v1
Checksum:i057E3866432DC786
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR378673 Genomic DNA. Translation: CAG21482.1.
RefSeqiYP_131284.1. NC_006370.1.

Genome annotation databases

EnsemblBacteriaiCAG21482; CAG21482; PBPRA3176.
GeneIDi3122642.
KEGGippr:PBPRA3176.
PATRICi22937417. VBIPhoPro109272_3324.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR378673 Genomic DNA. Translation: CAG21482.1 .
RefSeqi YP_131284.1. NC_006370.1.

3D structure databases

ProteinModelPortali Q6LMJ5.
SMRi Q6LMJ5. Positions 1-282.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 298386.PBPRA3176.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAG21482 ; CAG21482 ; PBPRA3176 .
GeneIDi 3122642.
KEGGi ppr:PBPRA3176.
PATRICi 22937417. VBIPhoPro109272_3324.

Phylogenomic databases

eggNOGi COG0414.
HOGENOMi HOG000175516.
KOi K01918.
OMAi HAGHMEL.
OrthoDBi EOG6Z6FZ4.

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00005 .
BioCyci PPRO298386-WGS:GSSB-3170-MONOMER.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_00158. PanC.
InterProi IPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
PANTHERi PTHR21299:SF1. PTHR21299:SF1. 1 hit.
Pfami PF02569. Pantoate_ligase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SS9.

Entry informationi

Entry nameiPANC_PHOPR
AccessioniPrimary (citable) accession number: Q6LMJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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