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Protein

PanD regulatory factor

Gene

panZ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD (PubMed:23170229, PubMed:25910242). Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA (PubMed:25910242).2 Publications

Enzyme regulationi

Activation of PanD processing occurs even at low CoA concentrations. In contrast, full inhibition of PanD catalytic activity only occurs at sufficiently high CoA concentrations.1 Publication

GO - Molecular functioni

GO - Biological processi

  • pantothenate biosynthetic process Source: EcoCyc
  • protein processing Source: EcoCyc
  • zymogen activation Source: EcoCyc

Keywordsi

Biological processPantothenate biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG12211-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
PanD regulatory factorUniRule annotationCurated
Gene namesi
Name:panZ1 PublicationUniRule annotation
Synonyms:panMBy similarityImported, yhhK
Ordered Locus Names:b3459, JW3424
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12211. panM.

Pathology & Biotechi

Disruption phenotypei

Deletion mutants are deficient in the biosynthetic pathway for pantothenate.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi45N → A: Loss of affinity for PanD. Is still able to activate but not regulate the PanD protein. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001695531 – 127PanD regulatory factorAdd BLAST127

Proteomic databases

PaxDbiP37613.
PRIDEiP37613.

Interactioni

Subunit structurei

Interacts with PanD in the presence of CoA (PubMed:23170229, PubMed:22940551, PubMed:25910242). Forms a heterooctameric complex composed of four PanD subunits and four PanZ subunits (PubMed:22940551, PubMed:25910242). Monomer in solution (PubMed:22940551).3 Publications

Protein-protein interaction databases

BioGridi4262496. 7 interactors.
IntActiP37613. 2 interactors.
STRINGi316385.ECDH10B_3633.

Structurei

Secondary structure

1127
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Helixi13 – 22Combined sources10
Beta strandi28 – 30Combined sources3
Beta strandi37 – 44Combined sources8
Beta strandi47 – 57Combined sources11
Beta strandi60 – 68Combined sources9
Helixi70 – 72Combined sources3
Beta strandi73 – 76Combined sources4
Helixi77 – 87Combined sources11
Beta strandi94 – 98Combined sources5
Helixi105 – 114Combined sources10
Beta strandi118 – 120Combined sources3
Beta strandi123 – 126Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K5TNMR-A1-127[»]
4CRYX-ray1.61B1-127[»]
4CRZX-ray1.70B1-127[»]
4CS0X-ray2.10B1-127[»]
5LS7X-ray1.16B1-127[»]
ProteinModelPortaliP37613.
SMRiP37613.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37613.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 127N-acetyltransferaseUniRule annotationAdd BLAST127

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni43 – 48Interaction with PanD1 Publication6
Regioni66 – 76Interaction with PanD1 PublicationAdd BLAST11
Regioni66 – 68Coenzyme A bindingUniRule annotationCombined sources3 Publications3
Regioni72 – 79Coenzyme A bindingUniRule annotationCombined sources3 Publications8

Sequence similaritiesi

Belongs to the PanZ/PanM family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105U59. Bacteria.
ENOG4111V7B. LUCA.
HOGENOMiHOG000125696.
InParanoidiP37613.

Family and domain databases

HAMAPiMF_02018. PanZ_PanM. 1 hit.
InterProiView protein in InterPro
IPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
IPR032900. PanM.
PfamiView protein in Pfam
PF12568. DUF3749. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiView protein in PROSITE
PS51186. GNAT. 1 hit.

Sequencei

Sequence statusi: Complete.

P37613-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLTIIRLEK FSDQDRIDLQ KIWPEYSPSS LQVDDNHRIY AARFNERLLA
60 70 80 90 100
AVRVTLSGTE GALDSLRVRE VTRRRGVGQY LLEEVLRNNP GVSCWWMADA
110 120
GVEDRGVMTA FMQALGFTAQ QGGWEKC
Length:127
Mass (Da):14,506
Last modified:October 1, 1994 - v1
Checksum:iEF054A30D294519A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18434.1.
U00096 Genomic DNA. Translation: AAC76484.1.
AP009048 Genomic DNA. Translation: BAE77834.1.
PIRiS47678.
RefSeqiNP_417916.1. NC_000913.3.
WP_000778768.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76484; AAC76484; b3459.
BAE77834; BAE77834; BAE77834.
GeneIDi947963.
KEGGiecj:JW3424.
eco:b3459.
PATRICifig|1411691.4.peg.3266.

Similar proteinsi

Entry informationi

Entry nameiPANZ_ECOLI
AccessioniPrimary (citable) accession number: P37613
Secondary accession number(s): Q2M7C2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 25, 2017
This is version 116 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Lacks the conserved catalytic glutamate found in many enzymatically active members of the Gcn5-like N-acetyltransferase (GNAT) family.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families