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O13907 (ACL2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable ATP-citrate synthase subunit 2
EC=2.3.3.8
Alternative name(s):
ATP-citrate (pro-S-)-lyase 2
Citrate cleavage enzyme subunit 2
Gene names
ORF Names:SPAC22A12.16
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA. Has a central role in de novo lipid synthesis By similarity.

Catalytic activity

ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA.

Subunit structure

Composed of two subunits By similarity.

Subcellular location

Cytoplasm. Nucleus Ref.2.

Sequence similarities

In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit family.

In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Probable ATP-citrate synthase subunit 2
PRO_0000340113

Amino acid modifications

Modified residue241Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
O13907 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 7B3FE2529B786CDA

FASTA49253,943
        10         20         30         40         50         60 
MSAKSIREYD GKAVLAYWLN RSPSISKEEY KTVSATPAVQ LAQIQFPLPT LVIPAESTTY 

        70         80         90        100        110        120 
REVVEDVFAK VEQEHPWVKE TKLVAKPDQL IKRRGKSGLL KLNATWDEAK EWIRERAGKN 

       130        140        150        160        170        180 
QKVQHAVGYL TTFLVEPFVP HPPNTEYYIN INSVREGDWI LFCNEGGVDV GDVDAKARKL 

       190        200        210        220        230        240 
LVPVRLSEFP SRATIASTLL SDIPVEQHES LVDFIIRLYS VYVDCQFTYL EINPLVVIPT 

       250        260        270        280        290        300 
AKGADVFYLD LAAKLDQTAE FECGAKWAVA RAPESLGIKT SGEESGAINA DHGPPMVFPA 

       310        320        330        340        350        360 
PFGRELSKEE AYVQGLDAKT GASLKLTILN AEGRVWNLVA GGGASVVYAD AVAVNGAADE 

       370        380        390        400        410        420 
LANYGEYSGA PTDGQTYEYA KTVLDLMTRG EPRADGKVLF IGGGIANFTS PAVTFRAIAR 

       430        440        450        460        470        480 
ALGDYKDKLH AHKVSIWVRR AGPNYQEGLR VIREAGKKFD LPLKVYGPEC HISGIVPMGL 

       490 
GKAPVEAEWQ MA

« Hide

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. expand/collapse author list , 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: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]"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-24, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAB16586.1.
PIRT38156.
RefSeqNP_593246.1. NM_001018643.1.

3D structure databases

ProteinModelPortalO13907.
ModBaseSearch...

Protein-protein interaction databases

STRINGO13907.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC22A12.16.1; SPAC22A12.16.1:pep; SPAC22A12.16.
GeneID2541811.
KEGGspo:SPAC22A12.16.
NMPDRfig|4896.1.peg.3216.

Organism-specific databases

GeneDB_SpombeSPAC22A12.16.

Phylogenomic databases

eggNOGfuNOG07699.
GeneTreeEFGT00050000003525.
HOGENOMHBG405181.
OMASVVYADA.
OrthoDBEOG415KNQ.

Gene expression databases

ArrayExpressO13907.

Family and domain databases

InterProIPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013816. ATP_grasp_subdomain_2.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
Gene3DG3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.40.50.261. Succinyl-CoA_synth-like. 1 hit.
KOK01648.
PfamPF08442. ATP-grasp_2. 1 hit.
[Graphical view]
SUPFAMSSF52210. CoA_ligase. 1 hit.
PROSITEPS01216. SUCCINYL_COA_LIG_1. False negative.
PS00399. SUCCINYL_COA_LIG_2. False negative.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACL2_SCHPO
AccessionPrimary (citable) accession number: O13907
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 1, 1998
Last modified: November 16, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents