Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A1KTB2

- PANC_NEIMF

UniProt

A1KTB2 - PANC_NEIMF

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pantothenate synthetase

Gene

panC

Organism
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
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.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei33 – 331Proton donorUniRule annotation
Binding sitei57 – 571Beta-alanineUniRule annotation
Binding sitei57 – 571PantoateUniRule annotation
Binding sitei150 – 1501PantoateUniRule annotation
Binding sitei173 – 1731ATP; via amide nitrogen and carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 338ATPUniRule annotation
Nucleotide bindingi144 – 1474ATPUniRule annotation
Nucleotide bindingi181 – 1844ATPUniRule annotation

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

BioCyciNMEN272831:GJDX-793-MONOMER.
UniPathwayiUPA00028; UER00005.

Names & Taxonomyi

Protein namesi
Recommended name:
Pantothenate synthetaseUniRule annotation (EC:6.3.2.1UniRule annotation)
Short name:
PSUniRule annotation
Alternative name(s):
Pantoate--beta-alanine ligaseUniRule annotation
Pantoate-activating enzymeUniRule annotation
Gene namesi
Name:panCUniRule annotation
Ordered Locus Names:NMC0812
OrganismiNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Taxonomic identifieri272831 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000002286: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 278278Pantothenate synthetasePRO_0000305495Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272831.NMC0812.

Structurei

3D structure databases

ProteinModelPortaliA1KTB2.
SMRiA1KTB2. Positions 1-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175516.
KOiK01918.
OMAiIHTIREL.
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.

A1KTB2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQIIHTIREL RAWRKNAGKV AFVPTMGNLH EGHLALVREA KKRADNVVVS
60 70 80 90 100
IFVNRLQFGQ GEDFDKYPRT LQQDADKLEA EGVAVVFAPD EKELYPNVEQ
110 120 130 140 150
RYSVEPPNLQ NELCGKFRPG HFLGVATVVS KLFNIVAPDV ACFGKKDYQQ
160 170 180 190 200
LAVIKGLTED LNFDVEIVPV DTGRAEDGLA LSSRNQYLSA AERDEAPRLY
210 220 230 240 250
RELKAVAESL AQGSLDYAGL EKRAVQSLTE YGWVVDYVEI RRADTLEVAR
260 270
AGDKKLVVLA AARLGTTRLI DNLEIKLP
Length:278
Mass (Da):31,021
Last modified:February 6, 2007 - v1
Checksum:i0BCB3F2C931B6DD9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM421808 Genomic DNA. Translation: CAM10095.1.
RefSeqiWP_011798849.1. NC_008767.1.
YP_974891.1. NC_008767.1.

Genome annotation databases

EnsemblBacteriaiCAM10095; CAM10095; NMC0812.
GeneIDi4675973.
KEGGinmc:NMC0812.
PATRICi20351451. VBINeiMen17609_0976.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM421808 Genomic DNA. Translation: CAM10095.1 .
RefSeqi WP_011798849.1. NC_008767.1.
YP_974891.1. NC_008767.1.

3D structure databases

ProteinModelPortali A1KTB2.
SMRi A1KTB2. Positions 1-277.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272831.NMC0812.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAM10095 ; CAM10095 ; NMC0812 .
GeneIDi 4675973.
KEGGi nmc:NMC0812.
PATRICi 20351451. VBINeiMen17609_0976.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00005 .
BioCyci NMEN272831:GJDX-793-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: ATCC 700532 / DSM 15464 / FAM18.

Entry informationi

Entry nameiPANC_NEIMF
AccessioniPrimary (citable) accession number: A1KTB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 6, 2007
Last modified: October 29, 2014
This is version 53 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.UniRule annotation

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