Skip Header

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

P43711

- FABH_HAEIN

UniProt

P43711 - FABH_HAEIN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

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

Gene

fabH

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - 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 annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei112 – 1121UniRule annotation
Active sitei243 – 2431UniRule annotation
Active sitei273 – 2731UniRule annotation

GO - Molecular functioni

  1. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: InterPro
  2. beta-ketoacyl-acyl-carrier-protein synthase III activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-HAMAP
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

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:HI_0157
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579: Chromosome

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3163163-oxoacyl-[acyl-carrier-protein] synthase 3PRO_0000110432Add
BLAST

Proteomic databases

PRIDEiP43711.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi71421.HI0157.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115
Beta strandi16 – 183
Helixi19 – 235
Helixi30 – 367
Beta strandi41 – 433
Helixi51 – 6616
Helixi70 – 723
Beta strandi75 – 795
Beta strandi86 – 883
Helixi90 – 978
Beta strandi104 – 1085
Helixi111 – 1133
Helixi114 – 12714
Beta strandi132 – 14110
Helixi142 – 1443
Turni151 – 1566
Beta strandi159 – 17113
Beta strandi174 – 1818
Beta strandi188 – 1903
Helixi208 – 22821
Turni229 – 2313
Turni234 – 2363
Beta strandi239 – 2424
Helixi247 – 25610
Helixi261 – 2633
Helixi268 – 2714
Helixi275 – 2773
Helixi278 – 28811
Beta strandi297 – 3048
Turni305 – 3073
Beta strandi308 – 3158

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IL3X-ray2.70A1-316[»]
ProteinModelPortaliP43711.
SMRiP43711. Positions 1-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43711.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni244 – 2485ACP-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.
KOiK00648.
OMAiAHIVEET.
OrthoDBiEOG6J74XN.
PhylomeDBiP43711.

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.

P43711-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNSRILSTGS YLPSHIRTNA DLEKMVDTSD EWIVTRSGIR ERRIAAEDET
60 70 80 90 100
VATMGFEAAK NAIEAAQINP QDIELIIVAT TSHSHAYPSA ACQVQGLLNI
110 120 130 140 150
DDAISFDLAA ACTGFVYALS VADQFIRAGK VKKALVIGSD LNSRKLDETD
160 170 180 190 200
RSTVVLFGDG AGAVILEASE QEGIISTHLH ASADKNNALV LAQPERGIEK
210 220 230 240 250
SGYIEMQGNE TFKLAVRELS NVVEETLLAN NLDKKDLDWL VPHQANLRII
260 270 280 290 300
TATAKKLEMD MSQVVVTLDK YANNSAATVP VALDEAIRDG RIQRGQLLLL
310
EAFGGGWTWG SALVRF
Length:316
Mass (Da):34,280
Last modified:November 1, 1995 - v1
Checksum:i2D00ADD61DCB6A66
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC21826.1.
PIRiF64051.
RefSeqiNP_438327.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC21826; AAC21826; HI_0157.
GeneIDi951067.
KEGGihin:HI0157.
PATRICi20188811. VBIHaeInf48452_0162.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC21826.1 .
PIRi F64051.
RefSeqi NP_438327.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IL3 X-ray 2.70 A 1-316 [» ]
ProteinModelPortali P43711.
SMRi P43711. Positions 1-316.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 71421.HI0157.

Chemistry

BindingDBi P43711.
ChEMBLi CHEMBL3822.

Proteomic databases

PRIDEi P43711.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC21826 ; AAC21826 ; HI_0157 .
GeneIDi 951067.
KEGGi hin:HI0157.
PATRICi 20188811. VBIHaeInf48452_0162.

Phylogenomic databases

eggNOGi COG0332.
KOi K00648.
OMAi AHIVEET.
OrthoDBi EOG6J74XN.
PhylomeDBi P43711.

Enzyme and pathway databases

UniPathwayi UPA00094 .

Miscellaneous databases

EvolutionaryTracei P43711.
PROi P43711.

Family and domain databases

Gene3Di 3.40.47.10. 2 hits.
HAMAPi MF_01815. FabH.
InterProi IPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view ]
SUPFAMi SSF53901. SSF53901. 1 hit.
TIGRFAMsi TIGR00747. fabH. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. "Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase III (FabH)."
    Khandekar S.S., Gentry D.R., Van Aller G.S., Warren P., Xiang H., Silverman C., Doyle M.L., Chambers P.A., Konstantinidis A.K., Brandt M., Daines R.A., Lonsdale J.T.
    J. Biol. Chem. 276:30024-30030(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION BY ANTIBIOTICS.

Entry informationi

Entry nameiFABH_HAEIN
AccessioniPrimary (citable) accession number: P43711
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Inhibited by the SB418011 antibiotic. Not inhibited by cerulenin, and weakly inhibited by thiolactomycin.

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3