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
Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 sitei128 – 1281UniRule annotation
Active sitei262 – 2621UniRule annotation
Active sitei292 – 2921UniRule 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

BioCyciMRAD426355:GJB5-4013-MONOMER.
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:Mrad2831_3968Imported
OrganismiMethylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831)Imported
Taxonomic identifieri426355 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium
ProteomesiUP000006589 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

STRINGi426355.Mrad2831_3968.

Structurei

3D structure databases

ProteinModelPortaliB1LZA0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni263 – 2675ACP-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.
OMAiAHIVEET.
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.

B1LZA0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLRTDPGQ HRRVPPLRSV VVGTGSSLPA RVVTNADLAE RVDTSDEWIV
60 70 80 90 100
QRTGIRQRHL AGPDETTSVL GTRAARAALD DAGLTADDID LVICATSTPD
110 120 130 140 150
HTFPATATQI QAALGIHQGA AFDLQAVCAG FVFAVSTADK FLTTGAARRA
160 170 180 190 200
LVIGAETFSR IVDWEDRTTC VLFGDGAGAV VLEAQEGAGD RGVLSASLRS
210 220 230 240 250
DGRHREKLYV DGGPGSTGTT GHLRMEGRDV FRFAVGQVTD VIVEAFAQAG
260 270 280 290 300
ITAEELDWFV PHQANRRIIE ASADKLGVAR DKIVLTVDRH GNTSAASIPL
310 320 330
ALDVARRDGR IRAGDLVMIE AIGGGFSWGA ALIRW
Length:335
Mass (Da):35,471
Last modified:April 29, 2008 - v1
Checksum:iF2251D22DA37780E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001001 Genomic DNA. Translation: ACB25942.1.
RefSeqiWP_012320899.1. NC_010505.1.
YP_001756625.1. NC_010505.1.

Genome annotation databases

EnsemblBacteriaiACB25942; ACB25942; Mrad2831_3968.
KEGGimrd:Mrad2831_3968.
PATRICi22576382. VBIMetRad70578_4064.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001001 Genomic DNA. Translation: ACB25942.1.
RefSeqiWP_012320899.1. NC_010505.1.
YP_001756625.1. NC_010505.1.

3D structure databases

ProteinModelPortaliB1LZA0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi426355.Mrad2831_3968.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACB25942; ACB25942; Mrad2831_3968.
KEGGimrd:Mrad2831_3968.
PATRICi22576382. VBIMetRad70578_4064.

Phylogenomic databases

eggNOGiCOG0332.
HOGENOMiHOG000246674.
KOiK00648.
OMAiAHIVEET.
OrthoDBiEOG6J74XN.

Enzyme and pathway databases

UniPathwayiUPA00094.
UPA00094.
BioCyciMRAD426355:GJB5-4013-MONOMER.

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

  1. "Complete sequence of chromosome of Methylobacterium radiotolerans JCM 2831."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.
    , Kyrpides N., Mikhailova N., Marx C.J., Richardson P.
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27329 / DSM 1819 / JCM 2831Imported.

Entry informationi

Entry nameiB1LZA0_METRJ
AccessioniPrimary (citable) accession number: B1LZA0
Entry historyi
Integrated into UniProtKB/TrEMBL: April 29, 2008
Last sequence update: April 29, 2008
Last modified: May 27, 2015
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

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.