Pyruvate formate-lyase 1-activating enzyme - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0A9N4 (PFLA_ECOLI)

Last modified June 16, 2009. Version 33. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Pyruvate formate-lyase 1-activating enzyme
    EC=1.97.1.4
Alternative name(s):
    PFL-activating enzyme 1
    Formate-C-acetyltransferase-activating enzyme 1

Gene names

Name:	pflA
Synonyms:	act
Ordered Locus Names:	b0902, JW0885

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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.
Catalytic activity	S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.
Cofactor	Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the organic radical-activating enzymes family.

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Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen and reactive oxygen species metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW [formate-C-acetyltransferase]-activating enzyme activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 246

245

Pyruvate formate-lyase 1-activating enzyme

PRO_0000200522

Sites

Metal binding

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Metal binding

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Metal binding

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A9N4-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 486E06A9CE97BF37
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FASTA

246

28,204

        10         20         30         40         50         60 
MSVIGRIHSF ESCGTVDGPG IRFITFFQGC LMRCLYCHNR DTWDTHGGKE VTVEDLMKEV 

        70         80         90        100        110        120 
VTYRHFMNAS GGGVTASGGE AILQAEFVRD WFRACKKEGI HTCLDTNGFV RRYDPVIDEL 

       130        140        150        160        170        180 
LEVTDLVMLD LKQMNDEIHQ NLVGVSNHRT LEFAKYLANK NVKVWIRYVV VPGWSDDDDS 

       190        200        210        220        230        240 
AHRLGEFTRD MGNVEKIELL PYHELGKHKW VAMGEEYKLD GVKPPKKETM ERVKGILEQY 


GHKVMF

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate-formate-lyase-activating enzyme deduced from the DNA nucleotide sequences." Roedel W., Plaga W., Frank R., Knappe J. Eur. J. Biochem. 177:153-158(1988) [PubMed: 3053170] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X08035 Genomic DNA. Translation: CAA30829.1.
U00096 Genomic DNA. Translation: AAC73988.1.
AP009048 Genomic DNA. Translation: BAA35637.1.

PIR

S01789.

RefSeq

AP_001532.1.
NP_415422.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3C8F	X-ray	2.25	A	2-246	[»]
3CB8	X-ray	2.77	A	2-246	[»]

ModBase

Search...

Genome annotation databases

GeneID

945517.

GenomeReviews

Gene locus JW0885 in contig AP009048_GR.
Gene locus b0902 in contig U00096_GR.

KEGG

ecj:JW0885.
eco:b0902.

Organism-specific databases

EchoBASE

EB0027.

EcoGene

EG10028. pflA.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A9N4.

OMA

P0A9N4. RFVVFMQ.

Enzyme and pathway databases

BioCyc

EcoCyc:PFLACTENZ-MON.

Family and domain databases

InterPro

IPR006638. Elp3/MiaB/NifB.
IPR012838. PFLA.
IPR001989. Radical_activat_CS.
IPR007197. Radical_SAM.
[Graphical view]

Pfam

PF04055. Radical_SAM. 1 hit.
[Graphical view]

SMART

SM00729. Elp3. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02493. PFLA. 1 hit.

PROSITE

PS01087. RADICAL_ACTIVATING. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

PFLA_ECOLI

Accession

Primary (citable) accession number: P0A9N4
Secondary accession number(s): P09374

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 33 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families