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Protein

Malonyl CoA-acyl carrier protein transacylase

Gene

fabD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei91 – 911By 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-UniPathway
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

BioCyciBSUB:BSU15900-MONOMER.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Malonyl CoA-acyl carrier protein transacylase (EC:2.3.1.39)
Short name:
MCT
Gene namesi
Name:fabD
Synonyms:ylpE
Ordered Locus Names:BSU15900
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU15900. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317Malonyl CoA-acyl carrier protein transacylasePRO_0000194210Add
BLAST

Proteomic databases

PaxDbiP71019.

Interactioni

Protein-protein interaction databases

IntActiP71019. 1 interaction.
MINTiMINT-8366726.
STRINGi224308.BSU15900.

Structurei

3D structure databases

ProteinModelPortaliP71019.
SMRiP71019. Positions 1-311.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FabD family.Curated

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000036504.
InParanoidiP71019.
KOiK00645.
OMAiPVVTNVE.
OrthoDBiEOG6W19KW.
PhylomeDBiP71019.

Family and domain databases

Gene3Di3.40.366.10. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR024925. Malonyl_CoA-ACP_transAc.
IPR004410. Malonyl_CoA-ACP_transAc_FabD.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000446. Mct. 1 hit.
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsiTIGR00128. fabD. 1 hit.

Sequencei

Sequence statusi: Complete.

P71019-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKIAFLFPG QGSQFIGMGK ELYEQVPAAK RLFDEADETL ETKLSSLIFE
60 70 80 90 100
GDAEELTLTY NAQPALLTTS IAVLEKFKES GITPDFTAGH SLGEYSALVA
110 120 130 140 150
AGALSFKDAV YTVRKRGEFM NEAVPAGEGA MAAILGMDAE ALKQVTDKVT
160 170 180 190 200
EEGNLVQLAN LNCPGQIVIS GTAKGVELAS ELAKENGAKR AIPLEVSGPF
210 220 230 240 250
HSELMKPAAE KLKEVLDACD IKDADVPVIS NVSADVMTEK ADIKEKLIEQ
260 270 280 290 300
LYSPVRFEES INKLIAEGVT TFIEIGPGKV LSGLVKKVNR RLKTIAVSDP
310
ETIELAIQTL KEENDNA
Length:317
Mass (Da):34,035
Last modified:May 30, 2000 - v2
Checksum:i191AE828B1C91D7F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1318VPAGEGAM → GCRLAKEQW(PubMed:8759840)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59433 Genomic DNA. Translation: AAC44306.1.
Y13937 Genomic DNA. Translation: CAA74249.1.
AL009126 Genomic DNA. Translation: CAB13463.1.
PIRiH69620.
RefSeqiNP_389472.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13463; CAB13463; BSU15900.
GeneIDi938488.
KEGGibsu:BSU15900.
PATRICi18974985. VBIBacSub10457_1684.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59433 Genomic DNA. Translation: AAC44306.1.
Y13937 Genomic DNA. Translation: CAA74249.1.
AL009126 Genomic DNA. Translation: CAB13463.1.
PIRiH69620.
RefSeqiNP_389472.1. NC_000964.3.

3D structure databases

ProteinModelPortaliP71019.
SMRiP71019. Positions 1-311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP71019. 1 interaction.
MINTiMINT-8366726.
STRINGi224308.BSU15900.

Proteomic databases

PaxDbiP71019.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13463; CAB13463; BSU15900.
GeneIDi938488.
KEGGibsu:BSU15900.
PATRICi18974985. VBIBacSub10457_1684.

Organism-specific databases

GenoListiBSU15900. [Micado]

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000036504.
InParanoidiP71019.
KOiK00645.
OMAiPVVTNVE.
OrthoDBiEOG6W19KW.
PhylomeDBiP71019.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciBSUB:BSU15900-MONOMER.

Family and domain databases

Gene3Di3.40.366.10. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR024925. Malonyl_CoA-ACP_transAc.
IPR004410. Malonyl_CoA-ACP_transAc_FabD.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000446. Mct. 1 hit.
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsiTIGR00128. fabD. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bacillus subtilis acyl carrier protein is encoded in a cluster of lipid biosynthesis genes."
    Morbidoni H.R., de Mendoza D., Cronan J.E. Jr.
    J. Bacteriol. 178:4794-4800(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168 genome."
    Foulger D., Errington J.
    Microbiology 144:801-805(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.

Entry informationi

Entry nameiFABD_BACSU
AccessioniPrimary (citable) accession number: P71019
Secondary accession number(s): O34463
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: January 7, 2015
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.