Beta-ketoacyl-ACP synthase II - Streptococcus pneumoniae

Preferred order of sections

Names and origin

Protein names

Submitted name:
Beta-ketoacyl-ACP synthase II EMBL AAF98276.1

Gene names

Name:

fabF EMBL AAF98276.1

Organism

Streptococcus pneumoniae EMBL AAF98276.1

Taxonomic identifier

1313 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family. RuleBase RU003694

Ontologies

Keywords
Ligand	Magnesium PDB 1OXH PDB 1OX0 PDB 2ALM Metal-binding PDB 1OXH PDB 1OX0 PDB 2ALM
Molecular function	Transferase RuleBase RU003694
Technical term	3D-structure PDB 1OXH PDB 1OX0 PDB 2ALM PDB 2RJT
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-ketoacyl-acyl-carrier-protein synthase II activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

301

1

Magnesium PDB 1OXH

Metal binding

302

1

Magnesium; via carbonyl oxygen PDB 1OXH

Metal binding

346

1

Magnesium PDB 1OXH

Metal binding

391

1

Magnesium PDB 1OXH

Metal binding

392

1

Magnesium; via carbonyl oxygen PDB 1OXH

Sequences

Sequence

Length

Mass (Da)

Tools

Q9FBC2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 976B8F9C7FDBD163
Show »

FASTA

411

43,932

        10         20         30         40         50         60 
MKLNRVVVTG YGVTSPIGNT PEEFWNSLAT GKIGIGGITK FDHSDFDVHN AAEIQDFPFD 

        70         80         90        100        110        120 
KYFVKKDTNR FDNYSLYALY AAQEAVNHAN LDVEALNRDR FGVIVASGIG GIKEIEDQVL 

       130        140        150        160        170        180 
RLHEKGPKRV KPMTLPKALP NMASGNVAMR FGANGVCKSI NTACSSSNDA IGDAFRSIKF 

       190        200        210        220        230        240 
GFQDVMLVGG TEASITPFAI AGFQALTALS TTEDPTRASI PFDKDRNGFV MGEGSGMLVL 

       250        260        270        280        290        300 
ESLEHAEKRG ATILAEVVGY GNTCDAYHMT SPHPEGQGAI KAIKLALEEA EISPEQVAYV 

       310        320        330        340        350        360 
NAHGTSTPAN EKGESGAIVA VLGKEVPVSS TKSFTGHLLG AAGAVEAIVT IEAMRHNFVP 

       370        380        390        400        410 
MTAGTSEVSD YIEANVVYGQ GLEKEIPYAI SNTFGFGGHN AVLAFKRWEN R

« Hide

References

[1]	"A triclosan-resistant bacterial enzyme." Heath R.J., Rock C.O. Nature 406:145-146(2000) [PubMed: 10910344] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: R6 EMBL AAF98276.1.
[2]	"The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae." Price A.C., Rock C.O., White S.W. J. Bacteriol. 185:4136-4143(2003) [PubMed: 12837788] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
[3]	"Roles of the active site water, histidine 303, and phenylalanine 396 in the catalytic mechanism of the elongation condensing enzyme of Streptococcus pneumoniae." Zhang Y.M., Hurlbert J., White S.W., Rock C.O. J. Biol. Chem. 281:17390-17399(2006) [PubMed: 16618705] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF197933 Genomic DNA. Translation: AAF98276.1.

PIR

H95048.

RefSeq

NP_344945.1. NC_003028.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OX0	X-ray	1.30	A	1-411	[»]
1OXH	X-ray	2.09	A/B/C/D	1-411	[»]
2ALM	X-ray	2.60	A	1-411	[»]
2RJT	X-ray	1.75	A/B/C/D	1-408	[»]

ProteinModelPortal

Q9FBC2.

SMR

Q9FBC2. Positions 1-409.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBSTRT00000026827; EBSTRP00000025919; EBSTRG00000026827.

GeneID

930358.

GenomeReviews

Gene locus SP_0422 in contig AE005672_GR.

KEGG

spn:SP_0422.

PATRIC

19705189. VBIStrPne105772_0440.

TIGR

SP_0422.

Phylogenomic databases

GeneTree

EBGT00050000027074.

HOGENOM

HBG757733.

OMA

NAQNTSQ.

ProtClustDB

PRK07314.

Enzyme and pathway databases

BioCyc

SPNE170187-1:SP_0422-MONOMER.

Family and domain databases

InterPro

IPR017568. 3-oxoacyl-ACP_synth-2.
IPR000794. Beta-ketoacyl_synthase.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]

Gene3D

G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.

KO

K09458.

PANTHER

PTHR11712. Ketoacyl_synth. 1 hit.

Pfam

PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000447. KAS_II. 1 hit.

SUPFAM

SSF53901. Thiolase-like. 2 hits.

TIGRFAMs

TIGR03150. FabF. 1 hit.

PROSITE

PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q9FBC2_STRPN

Accession

Primary (citable) accession number: Q9FBC2
Secondary accession number(s): Q7D4F8

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2001
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)