SubmitCancel

Skip Header

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

P0A9N5

- PFLA_ECOL6

UniProt

P0A9N5 - PFLA_ECOL6

(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
Pyruvate formate-lyase 1-activating enzyme
Gene
pflA, c1038
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine By similarity.

Catalytic activityi

S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.

Cofactori

Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi30 – 301Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal bindingi34 – 341Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal bindingi37 – 371Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. [formate-C-acetyltransferase]-activating enzyme activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. glucose metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate formate-lyase 1-activating enzyme (EC:1.97.1.4)
Alternative name(s):
Formate-C-acetyltransferase-activating enzyme 1
PFL-activating enzyme 1
Gene namesi
Name:pflA
Ordered Locus Names:c1038
OrganismiEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Taxonomic identifieri199310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001410: Chromosome

Subcellular locationi

Cytoplasm By similarity

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
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 246245Pyruvate formate-lyase 1-activating enzyme
PRO_0000200524Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi199310.c1038.

Structurei

3D structure databases

ProteinModelPortaliP0A9N5.
SMRiP0A9N5. Positions 2-246.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000011458.
KOiK04069.
OMAiDDASAHK.
OrthoDBiEOG64FKHC.

Family and domain databases

InterProiIPR006638. Elp3/MiaB/NifB.
IPR012838. PFL_activating.
IPR001989. Radical_activat_CS.
IPR007197. rSAM.
[Graphical view]
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02493. PFLA. 1 hit.
PROSITEiPS01087. RADICAL_ACTIVATING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A9N5-1 [UniParc]FASTAAdd to Basket

« Hide

MSVIGRIHSF ESCGTVDGPG IRFITFFQGC LMRCLYCHNR DTWDTHGGKE    50
VTVEDLMKEV VTYRHFMNAS GGGVTASGGE AILQAEFVRD WFRACKKEGI 100
HTCLDTNGFV RRYDPVIDEL LEVTDLVMLD LKQMNDEIHQ NLVGVSNHRT 150
LEFAKYLANK NVKVWIRYVV VPGWSDDDDS AHRLGEFTRD MGNVEKIELL 200
PYHELGKHKW VAMGEEYKLD GVKPPKKETM ERVKGILEQY GHKVMF 246
Length:246
Mass (Da):28,204
Last modified:January 23, 2007 - v2
Checksum:i486E06A9CE97BF37
GO

Sequence cautioni

The sequence AAN79510.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014075 Genomic DNA. Translation: AAN79510.1. Different initiation.
RefSeqiNP_752967.2. NC_004431.1.

Genome annotation databases

EnsemblBacteriaiAAN79510; AAN79510; c1038.
GeneIDi1038676.
KEGGiecc:c1038.
PATRICi18280119. VBIEscCol75197_0988.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014075 Genomic DNA. Translation: AAN79510.1 . Different initiation.
RefSeqi NP_752967.2. NC_004431.1.

3D structure databases

ProteinModelPortali P0A9N5.
SMRi P0A9N5. Positions 2-246.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 199310.c1038.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN79510 ; AAN79510 ; c1038 .
GeneIDi 1038676.
KEGGi ecc:c1038.
PATRICi 18280119. VBIEscCol75197_0988.

Phylogenomic databases

HOGENOMi HOG000011458.
KOi K04069.
OMAi DDASAHK.
OrthoDBi EOG64FKHC.

Family and domain databases

InterProi IPR006638. Elp3/MiaB/NifB.
IPR012838. PFL_activating.
IPR001989. Radical_activat_CS.
IPR007197. rSAM.
[Graphical view ]
Pfami PF04055. Radical_SAM. 1 hit.
[Graphical view ]
SMARTi SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02493. PFLA. 1 hit.
PROSITEi PS01087. RADICAL_ACTIVATING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CFT073 / ATCC 700928 / UPEC.

Entry informationi

Entry nameiPFLA_ECOL6
AccessioniPrimary (citable) accession number: P0A9N5
Secondary accession number(s): P09374
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi