P0A9N6 (PFLA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	pflA
Ordered Locus Names:	Z1246, ECs0985

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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 By similarity.
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 By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the organic radical-activating enzymes family.

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	Complete proteome
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 246	245	Pyruvate formate-lyase 1-activating enzyme		PRO_0000200523
Sites
	Metal binding	30	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	34	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	37	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A9N6 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 486E06A9CE97BF37	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

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG55387.1. BA000007 Genomic DNA. Translation: BAB34408.1.
PIR	A99752. G85615.
RefSeq	NP_286777.1. NC_002655.2. NP_309012.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P0A9N6.
SMR	P0A9N6. Positions 2-246.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000025924; EBESCP00000024817; EBESCG00000024977. EBESCT00000055714; EBESCP00000053542; EBESCG00000054762.
GeneID	917728. 958863.
GenomeReviews	Gene locus Z1246 in contig AE005174_GR. Gene locus ECs0985 in contig BA000007_GR.
KEGG	ece:Z1246. ecs:ECs0985.
PATRIC	18351227. VBIEscCol44059_1117.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009897.
HOGENOM	HBG554871.
OMA	LIGVPNK.
ProtClustDB	PRK11145.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS0985-MONOMER.
Family and domain databases
InterPro	IPR006638. Elp3/MiaB/NifB. IPR012838. PFL_activating. IPR001989. Radical_activat_CS. IPR007197. rSAM. [Graphical view]
KO	K04069.
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...

Entry information

Entry name

PFLA_ECO57

Accession

Primary (citable) accession number: P0A9N6
Secondary accession number(s): P09374

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program