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Q9R9J2

- FENF_BACIU

UniProt

Q9R9J2 - FENF_BACIU

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Protein
Malonyl CoA-acyl carrier protein transacylase
Gene
fenF
Organism
Bacillus subtilis
Status
Reviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Is involved in the mycosubtilin synthetase assembly, by catalyzing the transfer of malonyl groups to a specific acyl-carrier-protein domain on MycA.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=45 µM for malonyl-CoA1 Publication
  2. KM=950 µM for acyl-carrier-protein domain of MycA

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921 By similarity
Active sitei201 – 2011 By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Malonyl CoA-acyl carrier protein transacylase (EC:2.3.1.39)
Short name:
MCT
Gene namesi
Name:fenF
OrganismiBacillus subtilis
Taxonomic identifieri1423 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400Malonyl CoA-acyl carrier protein transacylase
PRO_0000385454Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9R9J2.

Family & Domainsi

Sequence similaritiesi

Belongs to the FabD family.

Family and domain databases

Gene3Di3.40.366.10. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR004410. Malonyl_CoA-ACP_transAc_FabD.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsiTIGR00128. fabD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9R9J2-1 [UniParc]FASTAAdd to Basket

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MNNLAFLFPG QGSQFVGMGK SFWNDFVLAK RLFEEASDAI SMDVKKLCFD    50
GDMTELTRTM NAQPAILTVS VIAYQVYMQE IGIKPHFLAG HSLGEYSALV 100
CAGVLSFQEA VKLIRQRGIL MQNADPEQLG TMAAITQVYI QPLQDLCTEI 150
STEDFPVGVA CMNSDQQHVI SGHRQAVEFV IKKAERMGAN HTYLNVSAPF 200
HSSMMRSASE QFQTALNQYS FRDAEWPIIS NVTAIPYNNG HSVREHLQTH 250
MTMPVRWAES MHYLLLHGVT EVIEMGPKNV LVGLLKKITN HIAAYPLGQT 300
SDLHLLSDSA ERNENIVNLR KKQLNKMMIQ SIIARNYNKD AKTYSNLTTP 350
LFPQIQLLKE RVERKEVELS AEELEHSIHL CQLICEAKQL PTWEQLRILK 400
Length:400
Mass (Da):45,222
Last modified:May 1, 2000 - v1
Checksum:i2A4430664C90C578
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF184956 Genomic DNA. Translation: AAF08794.1.
PIRiT44805.

Genome annotation databases

PATRICi37933545. VBIBacSub155824_1076.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF184956 Genomic DNA. Translation: AAF08794.1 .
PIRi T44805.

3D structure databases

ProteinModelPortali Q9R9J2.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

PATRICi 37933545. VBIBacSub155824_1076.

Family and domain databases

Gene3Di 3.40.366.10. 2 hits.
InterProi IPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR004410. Malonyl_CoA-ACP_transAc_FabD.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view ]
Pfami PF00698. Acyl_transf_1. 1 hit.
[Graphical view ]
SUPFAMi SSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsi TIGR00128. fabD. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The mycosubtilin synthetase of Bacillus subtilis ATCC6633: a multifunctional hybrid between a peptide synthetase, an amino transferase, and a fatty acid synthase."
    Duitman E.H., Hamoen L.W., Rembold M., Venema G., Seitz H., Saenger W., Bernhard F., Reinhardt R., Schmidt M., Ullrich C., Stein T., Leenders F., Vater J.
    Proc. Natl. Acad. Sci. U.S.A. 96:13294-13299(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 6633 / DSM 347 / IFO 3134 / PCI 219 / NRS 231.
  2. "FenF: servicing the mycosubtilin synthetase assembly line in trans."
    Aron Z.D., Fortin P.D., Calderone C.T., Walsh C.T.
    ChemBioChem 8:613-616(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: ATCC 6633 / DSM 347 / IFO 3134 / PCI 219 / NRS 231.

Entry informationi

Entry nameiFENF_BACIU
AccessioniPrimary (citable) accession number: Q9R9J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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