Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

Pathwayi: 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei123UniRule annotation1
Active sitei275UniRule annotation1
Active sitei306UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferaseUniRule annotationSAAS annotation, Transferase
Biological processFatty acid biosynthesisUniRule annotationSAAS annotation, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BRENDAi2.3.1.180. 3348.
UniPathwayiUPA00094.

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
Short name:
KAS 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
Proteomesi
  • UP000000738 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4EWPX-ray2.20A/B/C/D/E/F1-350[»]
ProteinModelPortaliC5CAR9.
SMRiC5CAR9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini117 – 194ACP_syn_IIIInterPro annotationAdd BLAST78
Domaini259 – 348ACP_syn_III_CInterPro annotationAdd BLAST90

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni276 – 280ACP-bindingUniRule annotation5

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 annotationSAAS annotation

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
HOGENOMiHOG000246674.
KOiK00648.
OMAiIGPTVWG.
OrthoDBiPOG091H02M9.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
HAMAPiMF_01815. FabH. 1 hit.
InterProiView protein in InterPro
IPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
PfamiView protein in Pfam
PF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
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.

Genome annotation databases

EnsemblBacteriaiACS30452; ACS30452; Mlut_09310.
GeneIDi7986167.
KEGGimlu:Mlut_09310.
PATRICifig|465515.4.peg.892.

Similar proteinsi

Entry informationi

Entry nameiC5CAR9_MICLC
AccessioniPrimary (citable) accession number: C5CAR9
Entry historyiIntegrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: September 27, 2017
This is version 65 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

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