O67185 (FABH_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3
EC=2.3.1.180

Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III
Beta-ketoacyl-ACP synthase III
Short name=KAS III

Gene names

Name:	fabH
Ordered Locus Names:	aq_1099

Organism

Aquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Aquificae › Aquificae › Aquificales › Aquificaceae › Aquifex › Aquifex aeolicus

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity. HAMAP-Rule MF_01815
Catalytic activity	Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP-Rule MF_01815
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01815
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Probable HAMAP-Rule MF_01815.
Domain	The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP-Rule MF_01815
Sequence similarities	Belongs to the FabH family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: InterPro beta-ketoacyl-acyl-carrier-protein synthase III activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 309

309

3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP-Rule MF_01815

PRO_0000110392

Regions

Region

237 – 241

5

ACP-binding By similarity

Sites

Active site

111

1

By similarity

Active site

236

1

By similarity

Active site

266

1

By similarity

Secondary structure

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309

Helix Strand Turn

Details...

Beta strand

3 – 11

9

Beta strand

14 – 18

5

Helix

19 – 23

5

Helix

30 – 37

8

Beta strand

41 – 44

4

Helix

50 – 65

16

Helix

69 – 71

3

Beta strand

73 – 78

6

Beta strand

83 – 87

5

Helix

89 – 97

9

Beta strand

103 – 108

6

Helix

110 – 112

3

Helix

113 – 126

14

Beta strand

131 – 140

10

Helix

141 – 143

3

Turn

150 – 155

6

Beta strand

158 – 167

10

Beta strand

169 – 171

3

Beta strand

173 – 181

9

Helix

183 – 188

6

Beta strand

189 – 191

3

Beta strand

197 – 199

3

Helix

201 – 223

23

Helix

227 – 229

3

Beta strand

231 – 235

5

Helix

240 – 249

10

Helix

254 – 256

3

Helix

261 – 264

4

Helix

268 – 270

3

Helix

271 – 281

11

Beta strand

290 – 297

8

Turn

298 – 300

3

Beta strand

301 – 308

8

Sequences

	Sequence		Length	Mass (Da)
	O67185 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: EB97518DB168140D	FASTA	309	33,825
	10 20 30 40 50 60 MGTKIIGTGV YLPKNVLTNF DLEKIVDTSD EWITTRTGIK ERRIAKEETI TYMATQAAKE 70 80 90 100 110 120 ALREANLSPE ELDLIILATL TPQKRFPSTA CLVQAQLKAK GVYAFDISAA CSGFIYALDI 130 140 150 160 170 180 ADSFIKSGKA KNVLVIGAEK LSEAVDWEDR STCVLFGDGA GAVVVTRSED KSDILATRMY 190 200 210 220 230 240 AEGSLEELLH ADNCGYIRMK GRELFKVAVR SMEEVCREVL EKAGVKPEEV SLVIPHQANV 250 260 270 280 290 300 RIINALAEKL NIPKEKVFVN IQKYGNTSAA SIPIALHEAI KEGKVKRGDL ILMTAMGGGL TWGAVLLRY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
[2]	"Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from Aquifex aeolicus VF5." RIKEN structural genomics initiative (RSGI) Submitted (AUG-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000657 Genomic DNA. Translation: AAC07144.1.

PIR

F70394.

RefSeq

NP_213748.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EBD	X-ray	2.10	A/B	1-309	[»]

ProteinModelPortal

O67185.

SMR

O67185. Positions 1-309.

ModBase

Search...

Protein-protein interaction databases

STRING

224324.aq_1099.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC07144; AAC07144; aq_1099.

GeneID

1193819.

KEGG

aae:aq_1099.

PATRIC

20959474. VBIAquAeo85532_0857.

Phylogenomic databases

eggNOG

COG0332.

HOGENOM

HOG000246674.

KO

K00648.

OMA

AHIVEET.

ProtClustDB

PRK09352.

Enzyme and pathway databases

BioCyc

AAEO224324:GJBH-783-MONOMER.

UniPathway

UPA00094.

Family and domain databases

Gene3D

3.40.47.10. 2 hits.

HAMAP

MF_01815. FabH.

InterPro

IPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]

Pfam

PF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]

SUPFAM

SSF53901. Thiolase-like. 1 hit.

TIGRFAMs

TIGR00747. fabH. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O67185.

Entry information

Entry name

FABH_AQUAE

Accession

Primary (citable) accession number: O67185

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program