P44422 (BIOF_HAEIN) 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:	HI_1553

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	380 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 Reference 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 – 380	380	Putative 8-amino-7-oxononanoate synthase		PRO_0000163813
Regions
	Region	106 – 107	2	Pyridoxal phosphate binding By similarity
	Region	205 – 208	4	Pyridoxal phosphate binding By similarity
	Region	236 – 239	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	18	1	Substrate By similarity
	Binding site	131	1	Substrate By similarity
	Binding site	179	1	Pyridoxal phosphate By similarity
	Binding site	352	1	Substrate By similarity
Amino acid modifications
	Modified residue	239	1	N6-(pyridoxal phosphate)lysine Probable

Sequences

	Sequence		Length	Mass (Da)
	P44422 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: B04083718BCEE470	FASTA	380	43,212
	10 20 30 40 50 60 MDAFKQQLEQ LSAKNQYRSI PDLVHQGRYI TRENRKMLNM SSNDYLGLAS NENLRQSFLQ 70 80 90 100 110 120 QYGGNFPSFT SSSSRLLTGN FPIYTDLEEL VAQRFQRESA LLFNSGYHAN IGILPALTTT 130 140 150 160 170 180 KSLILADKLV HASMIDGIRL SQCEFFRYRH NDYEHLKNLL EKNVGKFDRT FIVTESVFSM 190 200 210 220 230 240 DGDVADLKQL VQLKKQFPNT YLYVDEAHAV GVYGQNGLGI AERANVIADI DLLVGTFGKA 250 260 270 280 290 300 LASMGAYVVC DQILKECLIN QMRPLIFSTA LPPFNVAWTH FIFERLPQLS KERTHLEQLS 310 320 330 340 350 360 AFLRQEVEHR TQIMPSQTCI VPYILGENEA TLAKAKDLQE QGYYCLPIRP PTVPKNTSRI 370 380 RLSLTADMTA DEVRQFAVHL

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC23202.1.
PIR	D64129.
RefSeq	NP_439702.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P44422.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI1553.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC23202; AAC23202; HI_1553.
GeneID	950334.
KEGG	hin:HI1553.
PATRIC	20191831. VBIHaeInf48452_1624.
Phylogenomic databases
eggNOG	COG0156.
KO	K00652.
OMA	CLHAGNT.
ProtClustDB	PRK05958.
Enzyme and pathway databases
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_HAEIN

Accession

Primary (citable) accession number: P44422

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program