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P41398 (AK_CORFL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartokinase

EC=2.7.2.4
Alternative name(s):
Aspartate kinase
Gene names
Name:lysC
Synonyms:ask
OrganismCorynebacterium flavescens
Taxonomic identifier28028 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids lysine, threonine, isoleucine and methionine By similarity.

Catalytic activity

ATP + L-aspartate = ADP + 4-phospho-L-aspartate.

Enzyme regulation

Low feedback inhibition by lysine and threonine. The decreased sensitivity of C.flavum, as compared to C.glutamicum, is probably due to the Asp-345-Gly sequence difference. Ref.1

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.

Subunit structure

Tetramer consisting of 2 isoforms Alpha (catalytic and regulation) and of a homodimer of 2 isoforms Beta (regulation) By similarity.

Sequence similarities

Belongs to the aspartokinase family.

Contains 2 ACT domains.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Alpha (identifier: P41398-1)

Also known as: Aspartokinase subunit alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Beta (identifier: P41398-2)

Also known as: Aspartokinase subunit beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-249: Missing.
     250-250: V → M

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Aspartokinase
PRO_0000002377

Regions

Domain267 – 34377ACT 1
Domain349 – 42173ACT 2
Region7 – 104ATP binding By similarity
Region25 – 306Substrate binding By similarity
Region45 – 495Substrate binding By similarity
Region125 – 1262Substrate binding By similarity
Region151 – 1544Substrate binding By similarity
Region174 – 1752ATP binding By similarity
Region180 – 1856ATP binding By similarity
Region274 – 2796Substrate binding By similarity
Region292 – 2943Substrate binding By similarity
Region360 – 3612Substrate binding By similarity
Region374 – 3752Substrate binding By similarity
Region381 – 3822Substrate binding By similarity

Sites

Binding site411ATP By similarity
Binding site741Substrate By similarity
Binding site1541Substrate By similarity
Binding site2101ATP By similarity
Binding site2741Substrate By similarity
Binding site2981Substrate By similarity
Site71Contribution to the catalysis By similarity
Site741Contribution to the catalysis By similarity

Natural variations

Alternative sequence1 – 249249Missing in isoform Beta.
VSP_018657
Alternative sequence2501V → M in isoform Beta.
VSP_018658

Experimental info

Mutagenesis3451D → G: Decreased sensitivity of AK activity to concerted feedback inhibition by lysine and threonine. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha (Aspartokinase subunit alpha) [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 4B37B0B6597F665E

FASTA42144,797
        10         20         30         40         50         60 
MALVVQKYGG SSLESAERIR NVAERIVATK KAGNDVVVVC SAMGDTTDEL LELAAAVNPV 

        70         80         90        100        110        120 
PPAREMDMLL TAGERISNAL VAMAIESLGA EAQSFTGSQA GVLTTERHGN ARIVDVTPGR 

       130        140        150        160        170        180 
VREALDEGKI CIVAGFQGVN KETRDVTTLG RGGSDTTAVA LAAALNADVC EIYSDVDGVY 

       190        200        210        220        230        240 
TADPRIVPNA QKLEKLSFEE MLELAAVGSK ILVLRSVEYA RAFNVPLRVR SSYSNDPGTL 

       250        260        270        280        290        300 
IAGSMEDIPV EEAVLTGVAT DKSEAKVTVL GISDKPGEAA KVFRALADAE INIDMVLQNV 

       310        320        330        340        350        360 
SSVEDGTTDI TFTCPRADGR RAMEILKKLQ VQGNWTNVLY DDQVDKVSLV GAGMKSHPGV 

       370        380        390        400        410        420 
TAEFMEALRD VNVNIELIST SEIRISVLIR EDDLDAAARA LHEQFQLGGE DEAVVYAGTG 


R 

« Hide

Isoform Beta (Aspartokinase subunit beta) [UniParc].

Checksum: BC5043A4B488F0AF
Show »

FASTA17218,579

References

[1]"Gene structure and expression of the Corynebacterium flavum N13 ask-asd operon."
Follettie M.T., Peoples O.P., Agoropoulou C., Sinskey A.J.
J. Bacteriol. 175:4096-4103(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF ASP-345, ENZYME REGULATION.
Strain: N13.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L16848 Genomic DNA. Translation: AAA23293.1.

3D structure databases

ProteinModelPortalP41398.
SMRP41398. Positions 253-416.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00034; UER00015.
UPA00050; UER00461.
UPA00051; UER00462.

Family and domain databases

Gene3D3.40.1160.10. 1 hit.
InterProIPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR005260. Asp_kin_monofn.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
PF01842. ACT. 2 hits.
[Graphical view]
PIRSFPIRSF000726. Asp_kin. 1 hit.
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR00656. asp_kin_monofn. 1 hit.
TIGR00657. asp_kinases. 1 hit.
PROSITEPS51671. ACT. 2 hits.
PS00324. ASPARTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAK_CORFL
AccessionPrimary (citable) accession number: P41398
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 22, 2014
This is version 87 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

PATHWAY comments

Index of metabolic and biosynthesis pathways