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Protein

Malonyl CoA-acyl carrier protein transacylase, mitochondrial

Gene

mct1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Involved in biosynthesis of fatty acids in mitochondria.By similarity

Catalytic activityi

Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].

Pathwayi

GO - Molecular functioni

  1. [acyl-carrier-protein] S-malonyltransferase activity Source: PomBase

GO - Biological processi

  1. aerobic respiration Source: PomBase
  2. fatty acid biosynthetic process Source: UniProtKB-UniPathway
  3. fatty acid metabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Malonyl CoA-acyl carrier protein transacylase, mitochondrial (EC:2.3.1.39)
Short name:
MCT
Alternative name(s):
Malonyl-CoA:ACP transferase
Gene namesi
Name:mct1
ORF Names:SPAC11G7.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC11G7.05c.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 318Malonyl CoA-acyl carrier protein transacylase, mitochondrialPRO_0000314111
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

MaxQBiO13698.

Interactioni

Protein-protein interaction databases

MINTiMINT-4667256.
STRINGi4896.SPAC11G7.05c-1.

Structurei

3D structure databases

ProteinModelPortaliO13698.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FabD family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000036504.
InParanoidiO13698.
KOiK00645.
OMAiGDEHEIT.
OrthoDBiEOG7TBCFD.
PhylomeDBiO13698.

Family and domain databases

Gene3Di3.40.366.10. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O13698-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAILFPGQG VDWKTWMQPY LENNIVQNTL KEAENVTEIE IRKYIVEAEA
60 70 80 90 100
KSNLRQPITT IAQPAILACS IALLRAFPPF TKKFRFYVGH SLGEYSAFVA
110 120 130 140 150
SQTLSFSSAL KLVQARAKAM SYASALCQNP TSMLAITLTS RFPTDNFLNT
160 170 180 190 200
VYSAVQKYRL IDIANVNSDR QIVLSGDKKE LESITSTLSE LVRSLGKLRS
210 220 230 240 250
NWLDVSGAFH SRYMLPARDS LKNALGETEF NISPELCYTD SGKRFLPIIS
260 270 280 290 300
NVTAELYPAD EEDIRRQLLL QCFRPVLFKN CLKTVKSKYG ANLFYAYGPG
310
TTMQSIAKQN GISTKSRP
Length:318
Mass (Da):35,602
Last modified:January 1, 1998 - v1
Checksum:iC719BA7786333EE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16210.1.
PIRiT37548.
RefSeqiNP_594399.1. NM_001019822.2.

Genome annotation databases

EnsemblFungiiSPAC11G7.05c.1; SPAC11G7.05c.1:pep; SPAC11G7.05c.
GeneIDi2541662.
KEGGispo:SPAC11G7.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16210.1.
PIRiT37548.
RefSeqiNP_594399.1. NM_001019822.2.

3D structure databases

ProteinModelPortaliO13698.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4667256.
STRINGi4896.SPAC11G7.05c-1.

Proteomic databases

MaxQBiO13698.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC11G7.05c.1; SPAC11G7.05c.1:pep; SPAC11G7.05c.
GeneIDi2541662.
KEGGispo:SPAC11G7.05c.

Organism-specific databases

PomBaseiSPAC11G7.05c.

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000036504.
InParanoidiO13698.
KOiK00645.
OMAiGDEHEIT.
OrthoDBiEOG7TBCFD.
PhylomeDBiO13698.

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

NextBioi20802755.
PROiO13698.

Family and domain databases

Gene3Di3.40.366.10. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFABD_SCHPO
AccessioniPrimary (citable) accession number: O13698
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.