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Protein

3-oxoacyl-[acyl-carrier-protein] synthase 3

Gene

fabH

Organism
Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.UniRule annotation

Catalytic activityi

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2.UniRule annotationSAAS annotation

Pathway: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotationSAAS annotation
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Pathway: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei123 – 1231UniRule annotation
Active sitei275 – 2751UniRule annotation
Active sitei306 – 3061UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotationSAAS annotation, Transferase

Keywords - Biological processi

Fatty acid biosynthesisUniRule annotationSAAS annotation, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciMLUT465515:GHH6-929-MONOMER.
BRENDAi2.3.1.180. 3348.
UniPathwayiUPA00094.
UPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3UniRule annotation (EC:2.3.1.180UniRule annotation)
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase IIIUniRule annotation
Beta-ketoacyl-ACP synthase IIIUniRule annotation
Gene namesi
Name:fabHUniRule annotation
Ordered Locus Names:Mlut_09310Imported
OrganismiMicrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus)Imported
Taxonomic identifieri465515 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeMicrococcus
ProteomesiUP000000738 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi465515.MlutN2_010100002469.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EWPX-ray2.20A/B/C/D/E/F1-350[»]
ProteinModelPortaliC5CAR9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni276 – 2805ACP-bindingUniRule annotation

Domaini

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.UniRule annotation

Sequence similaritiesi

Belongs to the FabH family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0332.
HOGENOMiHOG000246674.
KOiK00648.
OrthoDBiEOG6J74XN.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
HAMAPiMF_01815. FabH.
InterProiIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 1 hit.
TIGRFAMsiTIGR00747. fabH. 1 hit.

Sequencei

Sequence statusi: Complete.

C5CAR9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVTLKQHER PAASRIVAVG AYRPANLVPN EDLIGPIDSS DEWIRQRTGI
60 70 80 90 100
VTRQRATAEE TVPVMAVGAA REALERAGLQ GSDLDAVIVS TVTFPHATPS
110 120 130 140 150
AAALVAHEIG ATPAPAYDVS AACAGYCYGV AQADALVRSG TARHVLVVGV
160 170 180 190 200
ERLSDVVDPT DRSISFLLGD GAGAVIVAAS DEPGISPSVW GSDGERWSTI
210 220 230 240 250
SMTHSQLELR DAVEHARTTG DASAITGAEG MLWPTLRQDG PSVFRWAVWS
260 270 280 290 300
MAKVAREALD AAGVEPEDLA AFIPHQANMR IIDEFAKQLK LPESVVVARD
310 320 330 340 350
IADAGNTSAA SIPLAMHRLL EENPELSGGL ALQIGFGAGL VYGAQVVRLP
Length:350
Mass (Da):36,749
Last modified:July 28, 2009 - v1
Checksum:i7CD8432B19C723B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001628 Genomic DNA. Translation: ACS30452.1.
RefSeqiWP_010078905.1. NZ_CABC01000032.1.
YP_002957006.1. NC_012803.1.

Genome annotation databases

EnsemblBacteriaiACS30452; ACS30452; Mlut_09310.
GeneIDi23699853.
KEGGimlu:Mlut_09310.
PATRICi22622508. VBIMicLut29563_0892.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001628 Genomic DNA. Translation: ACS30452.1.
RefSeqiWP_010078905.1. NZ_CABC01000032.1.
YP_002957006.1. NC_012803.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EWPX-ray2.20A/B/C/D/E/F1-350[»]
ProteinModelPortaliC5CAR9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi465515.MlutN2_010100002469.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACS30452; ACS30452; Mlut_09310.
GeneIDi23699853.
KEGGimlu:Mlut_09310.
PATRICi22622508. VBIMicLut29563_0892.

Phylogenomic databases

eggNOGiCOG0332.
HOGENOMiHOG000246674.
KOiK00648.
OrthoDBiEOG6J74XN.

Enzyme and pathway databases

UniPathwayiUPA00094.
UPA00094.
BioCyciMLUT465515:GHH6-929-MONOMER.
BRENDAi2.3.1.180. 3348.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
HAMAPiMF_01815. FabH.
InterProiIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 1 hit.
TIGRFAMsiTIGR00747. fabH. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230Imported.
  2. "Structure of FabH and factors affecting the distribution of branched fatty acids in Micrococcus luteus."
    Pereira J.H., Goh E.B., Keasling J.D., Beller H.R., Adams P.D.
    Acta Crystallogr. D 68:1320-1328(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).

Entry informationi

Entry nameiC5CAR9_MICLC
AccessioniPrimary (citable) accession number: C5CAR9
Entry historyi
Integrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: June 24, 2015
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Multifunctional enzymeUniRule annotationSAAS annotation, Reference proteomeImported

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.