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O68575 (PFLA_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Protein existenceInferred 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 263263Pyruvate formate-lyase-activating enzyme
PRO_0000200533

Sites

Metal binding371Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding411Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding441Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
O68575 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 575405F3EE248EFC

FASTA26330,150
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF051356 Genomic DNA. Translation: AAC05773.1.
AB018417 Genomic DNA. Translation: BAA34998.1.
AE014133 Genomic DNA. Translation: AAN59329.1.
RefSeqNP_722023.1. NC_004350.2.
YP_006490815.1. NC_018089.1.

3D structure databases

ProteinModelPortalO68575.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING210007.SMU.1692.

Protocols and materials databases

DNASU1028925.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN59329; AAN59329; SMU_1692.
GeneID1028925.
13299948.
KEGGsmu:SMU_1692.
smut:SMUGS5_07650.
PATRIC19665367. VBIStrMut61772_1512.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1180.
KOK04069.
OMAYVHSVES.
OrthoDBEOG64FKHC.
ProtClustDBCLSK876928.

Enzyme and pathway databases

BioCycSMUT210007:GC7Z-1584-MONOMER.

Family and domain databases

InterProIPR006638. Elp3/MiaB/NifB.
IPR012838. PFL_activating.
IPR001989. Radical_activat_CS.
IPR007197. rSAM.
[Graphical view]
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR02493. PFLA. 1 hit.
PROSITEPS01087. RADICAL_ACTIVATING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFLA_STRMU
AccessionPrimary (citable) accession number: O68575
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: November 13, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families