8-amino-7-oxononanoate synthase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P12998 (BIOF_ECOLI)

Last modified June 16, 2009. Version 87. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    8-amino-7-oxononanoate synthase
      Short name=AONS
    EC=2.3.1.47
Alternative name(s):
    8-amino-7-ketopelargonate synthase
    7-keto-8-amino-pelargonic acid synthetase
      Short name=7-KAP synthetase
    L-alanine--pimelyl-CoA ligase

Gene names

Name:	bioF
Ordered Locus Names:	b0776, JW0759

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	6-carboxyhexanoyl-CoA + L-alanine = 8-amino-7-oxononanoate + CoA + CO₂.
Cofactor	Pyridoxal phosphate.
Pathway	Cofactor biosynthesis; biotin biosynthesis; biotin from 6-carboxyhexanoyl-CoA: step 1/4.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

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Ontologies

Keywords
Biological process	Biotin biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	biotin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	8-amino-7-oxononanoate synthase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 384

384

8-amino-7-oxononanoate synthase

PRO_0000163811

Amino acid modifications

Modified residue

236

N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict

188 – 189

AE → R in CAA00968. Ref.2

Secondary structure

384

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P12998-1 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: D1AF5C054A5B4B06
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FASTA

384

41,594

        10         20         30         40         50         60 
MSWQEKINAA LDARRAADAL RRRYPVAQGA GRWLVADDRQ YLNFSSNDYL GLSHHPQIIR 

        70         80         90        100        110        120 
AWQQGAEQFG IGSGGSGHVS GYSVVHQALE EELAEWLGYS RALLFISGFA ANQAVIAAMM 

       130        140        150        160        170        180 
AKEDRIAADR LSHASLLEAA SLSPSQLRRF AHNDVTHLAR LLASPCPGQQ MVVTEGVFSM 

       190        200        210        220        230        240 
DGDSAPLAEI QQVTQQHNGW LMVDDAHGTG VIGEQGRGSC WLQKVKPELL VVTFGKGFGV 

       250        260        270        280        290        300 
SGAAVLCSST VADYLLQFAR HLIYSTSMPP AQAQALRASL AVIRSDEGDA RREKLAALIT 

       310        320        330        340        350        360 
RFRAGVQDLP FTLADSCSAI QPLIVGDNSR ALQLAEKLRQ QGCWVTAIRP PTVPAGTARL 

       370        380 
RLTLTAAHEM QDIDRLLEVL HGNG

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon." Otsuka A.J., Buoncristiani M.R., Howard P.K., Flamm J., Johnson O., Yamamoto R., Uchida K., Cook C., Ruppert J., Matsuzaki J. J. Biol. Chem. 263:19577-19585(1988) [PubMed: 3058702] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genetic material for expression of biotin synthetase enzymes." Pearson B.M., McKee R.A. Patent number GB2216530, 11-OCT-1989 Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme." Alexeev D., Alexeeva M., Baxter R.L., Campopiano D.J., Webster S.P., Sawyer L. J. Mol. Biol. 284:401-419(1998) [PubMed: 9813126] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

J04423 Genomic DNA. Translation: AAA23516.1.
A11542 Unassigned DNA. Translation: CAA00968.1.
U00096 Genomic DNA. Translation: AAC73863.1.
AP009048 Genomic DNA. Translation: BAE76363.1.

PIR

SYECKP. D32025.

RefSeq

AP_001407.1.
NP_415297.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BS0	X-ray	1.65	A	1-384	[»]
1DJ9	X-ray	2.00	A	1-384	[»]
1DJE	X-ray	1.71	A	1-384	[»]
2G6W	X-ray	2.14	A	1-384	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6870N.

Genome annotation databases

GeneID

945384.

GenomeReviews

Gene locus JW0759 in contig AP009048_GR.
Gene locus b0776 in contig U00096_GR.

KEGG

ecj:JW0759.
eco:b0776.

Organism-specific databases

EchoBASE

EB0119.

EcoGene

EG10121. bioF.

CMR

Search...

Phylogenomic databases

HOGENOM

P12998.

OMA

P12998. HAELEER.

Enzyme and pathway databases

BioCyc

EcoCyc:7KAPSYN-MON.
MetaCyc:7KAPSYN-MON.

Family and domain databases

InterPro

IPR004839. Aminotrans_I/II.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004723. BioF.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00858. bioF. 1 hit.

PROSITE

PS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

BIOF_ECOLI

Accession

Primary (citable) accession number: P12998
Secondary accession number(s): Q2MBJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	June 16, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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