Reviewed, UniProtKB/Swiss-Prot P43751 (PFLA_HAEIN)

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:	HI0179

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

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 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 246	245	Pyruvate formate-lyase 1-activating enzyme		PRO_0000200525
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)
	P43751-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 884313BD5B84376F	FASTA	246	28,235
	10 20 30 40 50 60 MSVLGRIHSF ESCGTVDGPG IRFILFMQGC LMRCKYCHNR DTWDLEGGKE ISVEDLMKEV 70 80 90 100 110 120 VTYRHFMNAT GGGVTASGGE AVLQAEFVRD WFRACKEEGI NTCLDTNGFV RHYDHIIDEL 130 140 150 160 170 180 LDVTDLVLLD LKELNDQVHQ NLIGVPNKRT LEFAKYLQKR NQHTWIRYVV VPGYTDSDHD 190 200 210 220 230 240 VHLLGQFIEG MTNIEKVELL PYHRLGVHKW KTLGLDYELE NVLPPTKESL EHIKTILEGY GHTVKF

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC21848.1.
PIR	E64052.
RefSeq	NP_438347.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	951086.
GenomeReviews	Gene locus HI0179 in contig L42023_GR.
KEGG	hin:HI0179.
NMPDR	fig|71421.1.peg.168.
TIGR	HI0179.
Phylogenomic databases
HOGENOM	P43751.
OMA	P43751. RFVVFMQ.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0179-MON.
BRENDA	1.97.1.4. 109.
Family and domain databases
InterPro	IPR012838. PFLA. IPR001989. Radical_activat_CS. IPR007197. Radical_SAM. [Graphical view]
Pfam	PF04055. Radical_SAM. 1 hit. [Graphical view]
TIGRFAMs	TIGR02493. PFLA. 1 hit.
PROSITE	PS01087. RADICAL_ACTIVATING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PFLA_HAEIN

Accession

Primary (citable) accession number: P43751

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 67 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)