3-oxoacyl-[acyl-carrier-protein] reductase FabG - Rickettsia prowazekii (strain Madrid E)

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P50941 (FABG_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] reductase FabG
EC=1.1.1.100

Alternative name(s):
3-ketoacyl-acyl carrier protein reductase
Beta-Ketoacyl-acyl carrier protein reductase
Beta-ketoacyl-ACP reductase

Gene names

Name:	fabG
Ordered Locus Names:	RP762

Organism

Rickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]

Taxonomic identifier

272947 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group ›

Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis By similarity.
Catalytic activity	(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP⁺ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homotetramer. Ref.4
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid elongation Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Inferred from sequence or structural similarity. Source: UniProtKB NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 241

241

3-oxoacyl-[acyl-carrier-protein] reductase FabG

PRO_0000054679

Regions

Nucleotide binding

13 – 16

NADP By similarity

Nucleotide binding

57 – 58

NADP By similarity

Nucleotide binding

148 – 152

NADP By similarity

Sites

Active site

148

Proton acceptor By similarity

Binding site

NADP By similarity

Binding site

NADP; via carbonyl oxygen By similarity

Binding site

135

Substrate By similarity

Binding site

181

NADP; via amide nitrogen and carbonyl oxygen By similarity

Secondary structure

241

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P50941 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: E43B8711545B8295
Show »

FASTA

241

25,759

        10         20         30         40         50         60 
MIDLTGKTSL ITGASSGIGS AIARLLHKLG SKVIISGSNE EKLKSLGNAL KDNYTIEVCN 

        70         80         90        100        110        120 
LANKEECSNL ISKTSNLDIL VCNAGITSDT LAIRMKDQDF DKVIDINLKA NFILNREAIK 

       130        140        150        160        170        180 
KMIQKRYGRI INISSIVGIA GNPGQANYCA SKAGLIGMTK SLSYEVATRG ITVNAVAPGF 

       190        200        210        220        230        240 
IKSDMTDKLN EKQREAIVQK IPLGTYGIPE DVAYAVAFLA SNNASYITGQ TLHVNGGMLM 


V

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Rickettsia prowazekii and the origin of mitochondria." Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G. Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Madrid E.
[2]	"Isolation and characterization of the Rickettsia prowazekii recA gene." Dunkin S.M., Winkler H.H., Wood D.O. J. Bacteriol. 176:1777-1781(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41. Strain: Madrid E.
[3]	"Codon usage and base composition in Rickettsia prowazekii." Andersson S.G.E., Sharp P.M. J. Mol. Evol. 42:525-536(1996) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[4]	"Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase rickettsia prowazekII." Joint center for strIuctural genomics (JCSG) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ235273 Genomic DNA. Translation: CAA15190.1.
U01959 Unassigned DNA. No translation available.

PIR

F71636.

RefSeq

NP_221114.1. NC_000963.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3F9I	X-ray	2.25	A/B	1-241	[»]

ProteinModelPortal

P50941.

ModBase

Search...

Protein-protein interaction databases

STRING

272947.RP762.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAA15190; CAA15190; CAA15190.

GeneID

883564.

KEGG

rpr:RP762.

PATRIC

17902389. VBIRicPro72556_0798.

Phylogenomic databases

eggNOG

COG1028.

K00059.

OMA

VEAHQGP.

ProtClustDB

PRK05653.

Enzyme and pathway databases

UniPathway

UPA00094.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR011284. 3oxo_ACP_reduc.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

TIGRFAMs

TIGR01830. 3oxo_ACP_reduc. 1 hit.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P50941.

Entry information

Entry name

FABG_RICPR

Accession

Primary (citable) accession number: P50941

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents