Reviewed, UniProtKB/Swiss-Prot P75794 (PFLE_ECOLI)

Names and origin

Protein names

Recommended name:
    Putative pyruvate formate-lyase 3-activating enzyme
    EC=1.97.1.4
Alternative name(s):
    PFL-activating enzyme 3
    Formate-C-acetyltransferase-activating enzyme 3

Gene names

Name:	ybiY
Ordered Locus Names:	b0824, JW0808

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	308 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Activation of pyruvate formate-lyase 2 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
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: InterPro 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 308	308	Putative pyruvate formate-lyase 3-activating enzyme		PRO_0000200528
Sites
	Metal binding	34	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	38	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	41	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P75794-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 21A5C573B7578A23	FASTA	308	34,139
	10 20 30 40 50 60 MLERNREATM IFNIQRYSTH DGPGIRTVVF LKGCSLGCRW CQNPESRART QDLLYDARLC 70 80 90 100 110 120 LEGCELCAKA APEVIERALN GLLIHREKLT PEHLTALTDC CPTQALTVCG EVKSVEEIMT 130 140 150 160 170 180 TVLRDKPFYD RSGGGLTLSG GEPFMQPEMA MALLQASHEA GIHTAVETCL HVPWKYIAPS 190 200 210 220 230 240 LPYIDLFLAD LKHVADAPFK QWTDGNAARV LDNLKKLAAA GKKIIIRVPL IQGFNADETS 250 260 270 280 290 300 VKAITDFAAD ELHVGEIHFL PYHTLGINKY HLLNLPYDAP EKPLDAPELL DFAQQYACQK GLTATLRG

References

[1]	"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. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., 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.
[2]	"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.
[3]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00096 Genomic DNA. Translation: AAC73911.1. AP009048 Genomic DNA. Translation: BAA35512.1.
PIR	H64819.
RefSeq	AP_001455.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:11444N.
Genome annotation databases
GenomeReviews	Gene locus JW0808 in contig AP009048_GR. Gene locus b0824 in contig U00096_GR.
KEGG	ecj:JW0808. eco:b0824.
Organism-specific databases
EchoBASE	EB3243.
EcoGene	EG13470. ybiY.
CMR	Search...
Phylogenomic databases
HOGENOM	P75794.
OMA	P75794. PRLCLEG.
Enzyme and pathway databases
BioCyc	EcoCyc:G6427-MON.
Family and domain databases
InterPro	IPR012839. Glycyl_radical_enz-activating. IPR011352. PFL_act_enz. IPR001989. Radical_activat_CS. IPR007197. Radical_SAM. [Graphical view]
Pfam	PF04055. Radical_SAM. 1 hit. [Graphical view]
PIRSF	PIRSF000371. PFL_act_enz. 1 hit.
TIGRFAMs	TIGR02494. PFLE_PFLC. 1 hit.
PROSITE	PS01087. RADICAL_ACTIVATING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PFLE_ECOLI

Accession

Primary (citable) accession number: P75794

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	June 16, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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