Reviewed, UniProtKB/Swiss-Prot O68575 (PFLA_STRMU)

Names and origin

Protein names

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

Gene names

Name:	act
Synonyms:	pflA, pflC
Ordered Locus Names:	SMU_1692

Organism

Streptococcus mutans [Complete proteome] [HAMAP]

Taxonomic identifier

1309 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	263 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 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 By similarity.
Subcellular location	Cytoplasm.
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	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 – 263	263	Pyruvate formate-lyase-activating enzyme		PRO_0000200533
Sites
	Metal binding	37	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	41	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	44	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O68575-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 575405F3EE248EFC	FASTA	263	30,150
	10 20 30 40 50 60 MIEKVDYEKV TGLVNSTESF GSVDGPGIRF VVFMQGCQMR CQYCHNPDTW AMKNDRATER 70 80 90 100 110 120 TAGDVFKEAL RFKDFWGDTG GITVSGGEAT LQMDFLIALF SLAKEKGIHT TLDTCALTFR 130 140 150 160 170 180 NTPKYLEKYE KLMAVTDLVL LDIKEINPDQ HKIVTGHSNK TILACARYLS DIGKPVWIRH 190 200 210 220 230 240 VLVPGLTDRD EDLIKLGEYV KTLKNVQRFE ILPYHTMGEF KWRELGIPYP LEGVKPPTPD 250 260 RVRNAKKLMH TETYEEYKKR INH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Defects in D-alanyl-lipoteichoic acid synthesis in Streptococcus mutans results in acid sensitivity." Boyd D.A., Cvitkovitch D.G., Bleiweis A.S., Kiriukhin M.Y., Debabov D.V., Neuhaus F.C., Hamilton I.R. J. Bacteriol. 182:6055-6065(2000) [PubMed: 11029425] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LT11.
[2]	"Characterization of the Streptococcus mutans pyruvate formate-lyase (PFL)-activating enzyme gene by complementary reconstitution of the in vitro PFL-reactivating system." Yamamoto Y., Sato Y., Takahashi-Abbe S., Takahashi N., Kizaki H. Infect. Immun. 68:4773-4777(2000) [PubMed: 10899886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: GS-5.
[3]	"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen." Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J. Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed: 12397186] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700610 / UA159 / Serotype c.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF051356 Genomic DNA. Translation: AAC05773.1. AB018417 Genomic DNA. Translation: BAA34998.1. AE014133 Genomic DNA. Translation: AAN59329.1.
RefSeq	NP_722023.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1028925.
GenomeReviews	Gene locus SMU_1692 in contig AE014133_GR.
KEGG	smu:SMU.1692.
NMPDR	fig|210007.1.peg.1536.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O68575.
OMA	O68575. RFVVFMQ.
Enzyme and pathway databases
BioCyc	SMUT210007:SMU_1692-MON.
BRENDA	1.97.1.4. 20716.
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...

Entry information

Entry name

PFLA_STRMU

Accession

Primary (citable) accession number: O68575

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	August 1, 1998
Last modified:	June 16, 2009
This is version 72 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)