Reviewed, UniProtKB/Swiss-Prot O60163 (AK_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable aspartokinase
    EC=2.7.2.4
Alternative name(s):
    Aspartate kinase

Gene names

ORF Names:

SPBC19F5.04

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	519 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; 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.
Sequence similarities	Belongs to the aspartokinase family. Contains 2 ACT domains.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Threonine biosynthesis
Domain	Repeat
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	amino acid binding Inferred from electronic annotation. Source: InterPro aspartate kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 519	519	Probable aspartokinase		PRO_0000066689
Regions
	Domain	359 – 431	73	ACT 1
	Domain	435 – 503	69	ACT 2
Amino acid modifications
	Modified residue	326	1	Phosphoserine
	Modified residue	328	1	Phosphothreonine

Sequences

	Sequence		Length	Mass (Da)
	O60163-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 0B392EB4AE8ECFCB	FASTA	519	56,813
	10 20 30 40 50 60 MSIAKNIEND PSKGWVVQKF GGTSVGKFPI KIAVDVAKEY LSTKRVALVC SARSTDTKAE 70 80 90 100 110 120 GTTTRLIRAT EAALRPAVGS VHDLVRIIET DHVQAARDFI QDVGIQDELI DAFHADCVEL 130 140 150 160 170 180 EQYLNAIRVL SEVSPRTRDL VIGMGERLSC RFMAAVLKDQ GIDSEFIDMS HIIDEQREWR 190 200 210 220 230 240 NLDASFYAYL ASQLASKVTA VGNKVPVVTG FFGMVPGGLL SQIGRGYTDF CAALLAVGLN 250 260 270 280 290 300 ADELQIWKEV DGIFTADPRK VPTARLLPLI TPEEAAELTY YGSEVIHPFT MSQVVHARIP 310 320 330 340 350 360 IRIKNVGNPR GKGTVIFPDT ISRHGSATPP HPPKIMPDDI SASLANKGAT AVTIKDTIMV 370 380 390 400 410 420 INIQSNRKIS AHGFLASIFA ILDKYKLAVD LITTSEVHVS MALYEESDDG NMHEAFVELR 430 440 450 460 470 480 RLGTLDILHG LAILSLVGKH MRNTTGYAGR MFCKLAEAQI NIEMISQGAS EINISCVIDE 490 500 510 KMAVKALNVI HKELLEPLAL HEVPSQASML VEKPWLYSA

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326 AND THR-328, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAA18652.1.
PIR	T39822.
RefSeq	NP_596542.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2540602.
KEGG	spo:SPBC19F5.04.
NMPDR	fig|4896.1.peg.2408.
Organism-specific databases
GeneDB_Spombe	SPBC19F5.04.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-004539-MON.
Gene expression databases
ArrayExpress	O60163.
Family and domain databases
InterPro	IPR002912. ACT_bd. IPR001048. Asp/Glu/Uridylate_kinase. IPR001341. Asp_kin_reg. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 1 hit.
Pfam	PF00696. AA_kinase. 1 hit. PF01842. ACT. 1 hit. [Graphical view]
TIGRFAMs	TIGR00657. asp_kinases. 1 hit.
PROSITE	PS00324. ASPARTOKINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AK_SCHPO

Accession

Primary (citable) accession number: O60163

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	August 1, 1998
Last modified:	November 25, 2008
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)