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Protein

Pyruvate formate-lyase-activating enzyme

Gene

act

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi37 – 371Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi41 – 411Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi44 – 441Iron-sulfur (4Fe-4S-S-AdoMet)By similarity

GO - Molecular functioni

  1. [formate-C-acetyltransferase]-activating enzyme activity Source: UniProtKB-EC
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciSMUT210007:GC7Z-1584-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate formate-lyase-activating enzyme (EC:1.97.1.4)
Short name:
PFL-activating enzyme
Alternative name(s):
Formate-C-acetyltransferase-activating enzyme
Gene namesi
Name:act
Synonyms:pflA, pflC
Ordered Locus Names:SMU_1692
OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
Taxonomic identifieri210007 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000002512 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263Pyruvate formate-lyase-activating enzymePRO_0000200533Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi210007.SMU.1692.

Structurei

3D structure databases

ProteinModelPortaliO68575.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1180.
KOiK04069.
OMAiRFVLFMQ.
OrthoDBiEOG64FKHC.
PhylomeDBiO68575.

Family and domain databases

InterProiIPR006638. Elp3/MiaB/NifB.
IPR012838. PFL_activating.
IPR001989. Radical_activat_CS.
IPR007197. rSAM.
[Graphical view]
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02493. PFLA. 1 hit.
PROSITEiPS01087. RADICAL_ACTIVATING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O68575-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIEKVDYEKV TGLVNSTESF GSVDGPGIRF VVFMQGCQMR CQYCHNPDTW
60 70 80 90 100
AMKNDRATER TAGDVFKEAL RFKDFWGDTG GITVSGGEAT LQMDFLIALF
110 120 130 140 150
SLAKEKGIHT TLDTCALTFR NTPKYLEKYE KLMAVTDLVL LDIKEINPDQ
160 170 180 190 200
HKIVTGHSNK TILACARYLS DIGKPVWIRH VLVPGLTDRD EDLIKLGEYV
210 220 230 240 250
KTLKNVQRFE ILPYHTMGEF KWRELGIPYP LEGVKPPTPD RVRNAKKLMH
260
TETYEEYKKR INH
Length:263
Mass (Da):30,150
Last modified:August 1, 1998 - v1
Checksum:i575405F3EE248EFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051356 Genomic DNA. Translation: AAC05773.1.
AB018417 Genomic DNA. Translation: BAA34998.1.
AE014133 Genomic DNA. Translation: AAN59329.1.
RefSeqiNP_722023.1. NC_004350.2.
WP_002262580.1. NC_004350.2.
YP_006490815.1. NC_018089.1.

Genome annotation databases

EnsemblBacteriaiAAN59329; AAN59329; SMU_1692.
GeneIDi1028925.
13299948.
KEGGismu:SMU_1692.
smut:SMUGS5_07650.
PATRICi19665367. VBIStrMut61772_1512.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051356 Genomic DNA. Translation: AAC05773.1.
AB018417 Genomic DNA. Translation: BAA34998.1.
AE014133 Genomic DNA. Translation: AAN59329.1.
RefSeqiNP_722023.1. NC_004350.2.
WP_002262580.1. NC_004350.2.
YP_006490815.1. NC_018089.1.

3D structure databases

ProteinModelPortaliO68575.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi210007.SMU.1692.

Protocols and materials databases

DNASUi1028925.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN59329; AAN59329; SMU_1692.
GeneIDi1028925.
13299948.
KEGGismu:SMU_1692.
smut:SMUGS5_07650.
PATRICi19665367. VBIStrMut61772_1512.

Phylogenomic databases

eggNOGiCOG1180.
KOiK04069.
OMAiRFVLFMQ.
OrthoDBiEOG64FKHC.
PhylomeDBiO68575.

Enzyme and pathway databases

BioCyciSMUT210007:GC7Z-1584-MONOMER.

Family and domain databases

InterProiIPR006638. Elp3/MiaB/NifB.
IPR012838. PFL_activating.
IPR001989. Radical_activat_CS.
IPR007197. rSAM.
[Graphical view]
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02493. PFLA. 1 hit.
PROSITEiPS01087. RADICAL_ACTIVATING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1999) [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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: GS-5.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700610 / UA159.

Entry informationi

Entry nameiPFLA_STRMU
AccessioniPrimary (citable) accession number: O68575
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: January 7, 2015
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.