A1U4B1 (BIOF_MARAV) 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
Short name=KAPA synthase
8-amino-7-ketopelargonate synthase

Gene names

Name:	bioF
Ordered Locus Names:	Maqu_2755

Organism

Marinobacter aquaeolei (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter hydrocarbonoclasticus (strain DSM 11845)) [Complete proteome] [HAMAP]

Taxonomic identifier

351348 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Alteromonadaceae › Marinobacter › Marinobacter hydrocarbonoclasticus

Protein attributes

Sequence length	394 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. HAMAP-Rule MF_01693
Catalytic activity	Pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]. HAMAP-Rule MF_01693
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Cofactor biosynthesis; biotin biosynthesis. HAMAP-Rule MF_01693
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: HAMAP
Molecular_function	8-amino-7-oxononanoate synthase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 394	394	8-amino-7-oxononanoate synthase HAMAP-Rule MF_01693		PRO_0000381017
Regions
	Region	105 – 106	2	Pyridoxal phosphate binding By similarity
	Region	200 – 203	4	Pyridoxal phosphate binding By similarity
	Region	232 – 235	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	18	1	Substrate By similarity
	Binding site	130	1	Substrate By similarity
	Binding site	175	1	Pyridoxal phosphate By similarity
	Binding site	349	1	Substrate By similarity
Amino acid modifications
	Modified residue	235	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1U4B1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 8B59A7064422299E	FASTA	394	42,038
	10 20 30 40 50 60 MRDFAKEIEQ RKQAGLYRTR RLIAGPQQPT LTADGRSLLS FCSNDYLGLA SHGENMRALE 70 80 90 100 110 120 QALPEVGLGG AASHLVCGHH EAHHRLEQRL AAFTRRSSAL FFSTGYMANM GVISALAGRG 130 140 150 160 170 180 DTIFSDRLNH ASIIDGCILS RARVRRYAHG DVAALETMLS ETSGHKLVVT DGVFSMDGDI 190 200 210 220 230 240 APLTELARVC KAHDALLVVD DAHGVGVLGP QGRGSVLEAG LCQEDVPVLI GTLGKGVGTS 250 260 270 280 290 300 GAFVAGSDVL IDYLVQKART YIYTTAMPPA LAAATCASLD AVESGDERRA HLDALIQRFR 310 320 330 340 350 360 AGAQDLGYEL MSSRTPIQPI MIGDNWTALA LSRALEDEGL LVTAIRPPTV PEGEARLRVT 370 380 390 LSAAHTEADV DRLLRALAKS RSVLSEAVAR EPAL

References

[1]

"Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Edwards K., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700491 / DSM 11845 / VT8.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000514 Genomic DNA. Translation: ABM19830.1.
RefSeq	YP_960017.1. NC_008740.1.
3D structure databases
ProteinModelPortal	A1U4B1.
ModBase	Search...
Protein-protein interaction databases
STRING	351348.Maqu_2755.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABM19830; ABM19830; Maqu_2755.
GeneID	4656017.
KEGG	maq:Maqu_2755.
PATRIC	22460856. VBIMarAqu65105_3170.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0156.
HOGENOM	HOG000221021.
KO	K00652.
OMA	ATVMAMS.
Enzyme and pathway databases
BioCyc	MHYD351348:GHYZ-2817-MONOMER.
UniPathway	UPA00078.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
HAMAP	MF_01693. BioF_aminotrans_2.
InterPro	IPR022834. Amino_oxononanoate_synth. 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_MARAV

Accession

Primary (citable) accession number: A1U4B1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	February 6, 2007
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program