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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].1 Publication

Kineticsi

  1. KM=45 µM for malonyl-CoA1 Publication
  2. KM=950 µM for acyl-carrier-protein domain of MycA1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921By similarity
Active sitei201 – 2011By 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 transacylasePRO_0000385454Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9R9J2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FabD family.Curated

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

« Hide

        10         20         30         40         50
MNNLAFLFPG QGSQFVGMGK SFWNDFVLAK RLFEEASDAI SMDVKKLCFD
60 70 80 90 100
GDMTELTRTM NAQPAILTVS VIAYQVYMQE IGIKPHFLAG HSLGEYSALV
110 120 130 140 150
CAGVLSFQEA VKLIRQRGIL MQNADPEQLG TMAAITQVYI QPLQDLCTEI
160 170 180 190 200
STEDFPVGVA CMNSDQQHVI SGHRQAVEFV IKKAERMGAN HTYLNVSAPF
210 220 230 240 250
HSSMMRSASE QFQTALNQYS FRDAEWPIIS NVTAIPYNNG HSVREHLQTH
260 270 280 290 300
MTMPVRWAES MHYLLLHGVT EVIEMGPKNV LVGLLKKITN HIAAYPLGQT
310 320 330 340 350
SDLHLLSDSA ERNENIVNLR KKQLNKMMIQ SIIARNYNKD AKTYSNLTTP
360 370 380 390 400
LFPQIQLLKE RVERKEVELS AEELEHSIHL CQLICEAKQL PTWEQLRILK
Length:400
Mass (Da):45,222
Last modified:May 1, 2000 - v1
Checksum:i2A4430664C90C578
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF184956 Genomic DNA. Translation: AAF08794.1.
PIRiT44805.

Genome annotation databases

PATRICi37933545. VBIBacSub155824_1076.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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: October 1, 2014
This is version 54 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