P22806 (BIOF_LYSSH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
8-amino-7-oxononanoate synthase
Short name=AONS
EC=2.3.1.47

Alternative name(s):
7-keto-8-amino-pelargonic acid synthase
Short name=7-KAP synthase
8-amino-7-ketopelargonate synthase

Gene names

Name:

bioF

Organism

Lysinibacillus sphaericus (Bacillus sphaericus)

Taxonomic identifier

1421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Lysinibacillus

Protein attributes

Sequence length	389 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide By similarity. Can also use pimeloyl-CoA instead of pimeloyl-ACP as substrate. Ref.2 Ref.3
Catalytic activity	Pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein].
Cofactor	Pyridoxal phosphate. Ref.2
Pathway	Cofactor biosynthesis; biotin biosynthesis.
Subunit structure	Homodimer. Ref.2
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.
Biophysicochemical properties	Kinetic parameters: KM=1.0 µM for pimeloyl-CoA (at pH 7.0 and at 37 degrees Celsius) Ref.2 KM=3.0 mM for L-alanine (at pH 7.0 and at 37 degrees Celsius)

Ontologies

Keywords
Biological process	Biotin biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	biotin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	8-amino-7-oxononanoate synthase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 389	389	8-amino-7-oxononanoate synthase		PRO_0000163808
Regions
	Region	106 – 107	2	Pyridoxal phosphate binding By similarity
	Region	203 – 206	4	Pyridoxal phosphate binding By similarity
	Region	234 – 237	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	19	1	Substrate By similarity
	Binding site	131	1	Substrate By similarity
	Binding site	178	1	Pyridoxal phosphate By similarity
	Binding site	351	1	Substrate By similarity
Amino acid modifications
	Modified residue	237	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P22806 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 7808F3A1A57EB5F6	FASTA	389	42,531
	10 20 30 40 50 60 MNDRFRRELQ VIEEQGLTRK LRLFSTGNES EVVMNGKKFL LFSSNNYLGL ATDSRLKKKA 70 80 90 100 110 120 TEGISKYGTG AGGSRLTTGN FDIHEQLESE IADFKKTEAA IVFSSGYLAN VGVISSVMKA 130 140 150 160 170 180 GDTIFSDAWN HASIIDGCRL SKAKTIVYEH ADMVDLERKL RQSHGDGLKF IVTDGVFSMD 190 200 210 220 230 240 GDIAPLPKIV ELAKEYKAYI MIDDAHATGV LGNDGCGTAD YFGLKDEIDF TVGTLSKAIG 250 260 270 280 290 300 AEGGFVSTSS IAKNYLLNNA RSFIFQTALS PSAIEAAREG ISIIQNEPER RKQLLKNAQY 310 320 330 340 350 360 LRLKLEESGF VMKEGETPII SLIIGGSHEA MQFSAKLLDE GVFIPAIRPP TVPKGSSRLR 370 380 ITVMATHTIE QLDMVISKIK KIGKEMGIV

References

[1]	"Cloning and characterization of the Bacillus sphaericus genes controlling the bioconversion of pimelate into dethiobiotin." Gloeckler R., Ohsawa I., Speck D., Ledoux C., Bernard S., Zinsius M., Villeval D., Kisou T., Kamogawa K., Lemoine Y. Gene 87:63-70(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10208 / NRS 966 / NCIB 11935 / 1911.
[2]	"The 8-amino-7-oxopelargonate synthase from Bacillus sphaericus. Purification and preliminary characterization of the cloned enzyme overproduced in Escherichia coli." Ploux O., Marquet A. Biochem. J. 283:327-331(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-14, FUNCTION AS A 8-AMINO-7-OXONONANOATE SYNTHASE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
[3]	"Mechanistic studies on the 8-amino-7-oxopelargonate synthase, a pyridoxal-5'-phosphate-dependent enzyme involved in biotin biosynthesis." Ploux O., Marquet A. Eur. J. Biochem. 236:301-308(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, REACTION MECHANISM.
[4]	"Crystallization and preliminary X-ray study of the 8-amino-7-oxopelargonate synthase from Bacillus sphaericus." Spinelli S., Ploux O., Marquet A., Anguille C., Jelsch C., Cambillau C., Martinez C. Acta Crystallogr. D 52:866-868(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M29291 Genomic DNA. Translation: AAA22271.1.
PIR	JQ0512.
3D structure databases
ProteinModelPortal	P22806.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14018.
SABIO-RK	P22806.
UniPathway	UPA00078.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR004723. BioF. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR00858. bioF. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BIOF_LYSSH

Accession

Primary (citable) accession number: P22806

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program