Adenosylmethionine-8-amino-7-oxononanoate aminotransferase

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Reviewed, UniProtKB/Swiss-Prot P12995 (BIOA_ECOLI)

Last modified June 16, 2009. Version 96. 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:
    Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
    EC=2.6.1.62
Alternative name(s):
    7,8-diamino-pelargonic acid aminotransferase
      Short name=DAPA aminotransferase

Gene names

Name:	bioA
Ordered Locus Names:	b0774, JW0757

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	429 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	S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate.
Cofactor	Pyridoxal phosphate.
Pathway	Cofactor biosynthesis; biotin biosynthesis; biotin from 6-carboxyhexanoyl-CoA: step 2/4.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

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Ontologies

Keywords
Biological process	Biotin biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate S-adenosyl-L-methionine
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	biotin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding 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 – 429

429

Adenosylmethionine-8-amino-7-oxononanoate aminotransferase

PRO_0000120366

Amino acid modifications

Modified residue

274

N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict

R → P in CAA00964. Ref.2

Sequence conflict

99 – 102

TPQP → SGRNA in AAA23514. Ref.1

Secondary structure

429

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P12995-1 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 84D2D1AE3A1280FF
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FASTA

429

47,336

        10         20         30         40         50         60 
MTTDDLAFDQ RHIWHPYTSM TSPLPVYPVV SAEGCELILS DGRRLVDGMS SWWAAIHGYN 

        70         80         90        100        110        120 
HPQLNAAMKS QIDAMSHVMF GGITHAPAIE LCRKLVAMTP QPLECVFLAD SGSVAVEVAM 

       130        140        150        160        170        180 
KMALQYWQAK GEARQRFLTF RNGYHGDTFG AMSVCDPDNS MHSLWKGYLP ENLFAPAPQS 

       190        200        210        220        230        240 
RMDGEWDERD MVGFARLMAA HRHEIAAVII EPIVQGAGGM RMYHPEWLKR IRKICDREGI 

       250        260        270        280        290        300 
LLIADEIATG FGRTGKLFAC EHAEIAPDIL CLGKALTGGT MTLSATLTTR EVAETISNGE 

       310        320        330        340        350        360 
AGCFMHGPTF MGNPLACAAA NASLAILESG DWQQQVADIE VQLREQLAPA RDAEMVADVR 

       370        380        390        400        410        420 
VLGAIGVVET THPVNMAALQ KFFVEQGVWI RPFGKLIYLM PPYIILPQQL QRLTAAVNRA 


VQDETFFCQ

« 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]	"Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes." Kack H., Sandmark J., Gibson K., Schneider G., Lindqvist Y. J. Mol. Biol. 291:857-876(1999) [PubMed: 10452893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

J04423 Genomic DNA. Translation: AAA23514.1.
A11524 Unassigned DNA. Translation: CAA00964.1.
U00096 Genomic DNA. Translation: AAC73861.1.
AP009048 Genomic DNA. Translation: BAE76361.1.

PIR

XNECDP. F64813.

RefSeq

AP_001405.1.
NP_415295.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DTY	X-ray	2.14	A/B	1-429	[»]
1MGV	X-ray	2.10	A/B	1-429	[»]
1MLY	X-ray	1.81	A/B	1-429	[»]
1MLZ	X-ray	2.15	A/B	1-429	[»]
1QJ3	X-ray	2.70	A/B	1-429	[»]
1QJ5	X-ray	1.80	A/B	1-429	[»]
1S06	X-ray	2.20	A/B	1-429	[»]
1S07	X-ray	2.42	A/B	1-429	[»]
1S08	X-ray	2.10	A/B	1-429	[»]
1S09	X-ray	1.83	A/B	1-429	[»]
1S0A	X-ray	1.71	A/B	1-429	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9219N.

Genome annotation databases

GeneID

945376.

GenomeReviews

Gene locus JW0757 in contig AP009048_GR.
Gene locus b0774 in contig U00096_GR.

KEGG

ecj:JW0757.
eco:b0774.

Organism-specific databases

EchoBASE

EB0115.

EcoGene

EG10117. bioA.

CMR

Search...

Phylogenomic databases

HOGENOM

P12995.

OMA

P12995. WQHQVAA.

Enzyme and pathway databases

BioCyc

EcoCyc:DAPASYN-MON.
MetaCyc:DAPASYN-MON.

BRENDA

2.6.1.62. 246.

Family and domain databases

InterPro

IPR005814. Aminotrans_3.
IPR005815. BioA.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.

PANTHER

PTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF8. BioA. 1 hit.

Pfam

PF00202. Aminotran_3. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00508. bioA. 1 hit.

PROSITE

PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

BIOA_ECOLI

Accession

Primary (citable) accession number: P12995
Secondary accession number(s): Q2MBJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 96 of the entry and version 2 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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