Q3A3Z8 (BIOF_PELCD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative 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
Ordered Locus Names:	Pcar_1665

Organism

Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1) [Complete proteome] [HAMAP]

Taxonomic identifier

338963 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Desulfuromonadales › Pelobacteraceae › Pelobacter › Pelobacter carbinolicus

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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.
Catalytic activity	Pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein].
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Cofactor biosynthesis; biotin biosynthesis.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.

Ontologies

Keywords
Biological process	Biotin biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Transferase
Technical term	Complete proteome
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 – 390	390	Putative 8-amino-7-oxononanoate synthase		PRO_0000381061
Regions
	Region	107 – 108	2	Pyridoxal phosphate binding By similarity
	Region	206 – 209	4	Pyridoxal phosphate binding By similarity
	Region	237 – 240	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	20	1	Substrate By similarity
	Binding site	132	1	Substrate By similarity
	Binding site	181	1	Pyridoxal phosphate By similarity
	Binding site	356	1	Substrate By similarity
Amino acid modifications
	Modified residue	240	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3A3Z8 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: 0E0731423FAC1A1D	FASTA	390	42,038
	10 20 30 40 50 60 MKLDHWQKTL DHLRDEEMLR GLKTVSGAQR DHVLLDGKDV LLLCSNNYLG LADHPALIEA 70 80 90 100 110 120 TCRATRDCGT GTGASRLVSG SMALHEELES KLAQFKGTQR ALLFNAGYAA NTGILQGLMG 130 140 150 160 170 180 ADDVIFSDSL NHASIIDGCR LSRAKTVVYP HRDTHALERL MAKEAPLRKG QWLIVTDGVF 190 200 210 220 230 240 SMDGDLAPLP ELVALKKRYD CLLMVDDAHG TGVLGDSGKG TGEYLGCLTD IDLHMGTLGK 250 260 270 280 290 300 ALGGFGAFVA GPDVVVQFLI NRARSFIFST SLPPGVVAAG IAALDIVNGS EGRQRRMNLQ 310 320 330 340 350 360 KLCTLFTGQL TESLPPEVRG ETPIVPILTG DPEPTMRASA WLEAQGIFVQ GIRPPTVPQG 370 380 390 RCRLRATLMA THQVEDLLRA ADLIRKVLSA

References

[1]

"Complete sequence of Pelobacter carbinolicus DSM 2380." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P. Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 2380 / Gra Bd 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000142 Genomic DNA. Translation: ABA88909.1.
RefSeq	YP_006717396.1. NC_007498.2.
3D structure databases
ProteinModelPortal	Q3A3Z8.
ModBase	Search...
Protein-protein interaction databases
STRING	338963.Pcar_1665.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABA88909; ABA88909; Pcar_1665.
GeneID	3724368.
KEGG	pca:Pcar_1665.
PATRIC	22889504. VBIPelCar86875_1811.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0156.
HOGENOM	HOG000221021.
KO	K00652.
OMA	VQGIRPP.
Enzyme and pathway databases
BioCyc	PCAR338963:GKDU-1846-MONOMER.
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_PELCD

Accession

Primary (citable) accession number: Q3A3Z8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	November 22, 2005
Last modified:	May 29, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program