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P12995

- BIOA_ECOLI

UniProt

P12995 - BIOA_ECOLI

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Protein

Adenosylmethionine-8-amino-7-oxononanoate aminotransferase

Gene

bioA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate.

Cofactori

pyridoxal 5'-phosphate1 Publication

Enzyme regulationi

Inhibited by amiclenomycin. S-adenosyl-L-(2-hydroxy-4-methylthio)butyric acid and adenosine are competitive inhibitors with SAM and uncompetitive inhibitors with KAPA as substrates. S-adenosyl-L-ethionine, adenine and 8-keto-7-aminopelargonic acid are non-competitive inhibitors with both substrates.3 Publications

Kineticsi

  1. KM=1.2 µM for KAPA2 Publications
  2. KM=150 µM for SAM2 Publications
  3. KM=21 µM for pyridoxamine phosphate (PMP)2 Publications
  4. KM=32 µM for pyridoxal phosphate (PLP)2 Publications
  5. KM=1000 µM for 8-keto-7-aminopelargonic acid2 Publications

Vmax=0.16 µmol/min/mg enzyme with KAPA as substrate2 Publications

Vmax=0.027 µmol/min/mg enzyme with 8-keto-7-aminopelargonic acid as substrate2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei17 – 171Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAMCurated
Binding sitei52 – 521Substrate1 Publication
Binding sitei144 – 1441Substrate1 Publication
Binding sitei245 – 2451Pyridoxal phosphate3 Publications
Binding sitei274 – 2741Substrate1 Publication
Binding sitei307 – 3071Substrate; via carbonyl oxygen1 Publication
Binding sitei391 – 3911Substrate1 Publication

GO - Molecular functioni

  1. adenosylmethionine-8-amino-7-oxononanoate transaminase activity Source: UniProtKB
  2. pyridoxal phosphate binding Source: UniProtKB

GO - Biological processi

  1. biotin biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Biotin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciEcoCyc:DAPASYN-MONOMER.
ECOL316407:JW0757-MONOMER.
MetaCyc:DAPASYN-MONOMER.
BRENDAi2.6.1.62. 2026.
SABIO-RKP12995.
UniPathwayiUPA00078; UER00160.

Names & Taxonomyi

Protein namesi
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 AT
Short name:
DAPA aminotransferase
7,8-diaminononanoate synthase
Short name:
DANS
Diaminopelargonic acid synthase
Gene namesi
Name:bioA
Ordered Locus Names:b0774, JW0757
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10117. bioA.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171Y → F: Severely reduces the aminotransferase activity. 1 Publication
Mutagenesisi144 – 1441Y → F: Severely reduces the aminotransferase activity. 1 Publication
Mutagenesisi147 – 1471D → N: Loss of aminotransferase activity. 1 Publication
Mutagenesisi253 – 2531R → A: Has only a small effect on the rate of reaction with DAPA. 1 Publication
Mutagenesisi253 – 2531R → K: Increases aminotransferase activity toward SAM. 1 Publication
Mutagenesisi253 – 2531R → M: Loss of aminotransferase activity. 1 Publication
Mutagenesisi253 – 2531R → Q: Increases aminotransferase activity toward SAM. 1 Publication
Mutagenesisi391 – 3911R → A: Reduces aminotransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Adenosylmethionine-8-amino-7-oxononanoate aminotransferasePRO_0000120366Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei274 – 2741N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiP12995.
PRIDEiP12995.

Expressioni

Inductioni

Repressed by BirA.1 Publication

Gene expression databases

GenevestigatoriP12995.

Interactioni

Subunit structurei

Homodimer.5 Publications

Protein-protein interaction databases

DIPiDIP-9219N.
IntActiP12995. 5 interactions.
MINTiMINT-1275136.
STRINGi511145.b0774.

Structurei

Secondary structure

1
429
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210Combined sources
Beta strandi20 – 223Combined sources
Beta strandi27 – 348Combined sources
Beta strandi36 – 394Combined sources
Beta strandi44 – 496Combined sources
Turni50 – 545Combined sources
Helixi62 – 7413Combined sources
Beta strandi81 – 844Combined sources
Helixi86 – 9813Combined sources
Beta strandi105 – 1117Combined sources
Helixi112 – 13019Combined sources
Beta strandi136 – 1405Combined sources
Helixi149 – 1524Combined sources
Turni157 – 1615Combined sources
Helixi162 – 1654Combined sources
Turni166 – 1683Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi180 – 1845Combined sources
Helixi188 – 1914Combined sources
Helixi192 – 20110Combined sources
Turni202 – 2043Combined sources
Beta strandi205 – 2106Combined sources
Beta strandi212 – 2154Combined sources
Turni217 – 2193Combined sources
Beta strandi221 – 2233Combined sources
Helixi226 – 23813Combined sources
Beta strandi241 – 2455Combined sources
Turni247 – 2548Combined sources
Beta strandi255 – 2584Combined sources
Helixi259 – 2635Combined sources
Beta strandi268 – 2725Combined sources
Helixi274 – 2774Combined sources
Beta strandi279 – 2813Combined sources
Beta strandi284 – 2885Combined sources
Helixi290 – 2978Combined sources
Beta strandi299 – 3035Combined sources
Turni309 – 3124Combined sources
Helixi314 – 32815Combined sources
Helixi332 – 34716Combined sources
Helixi348 – 3525Combined sources
Beta strandi356 – 3627Combined sources
Beta strandi365 – 3728Combined sources
Helixi376 – 38510Combined sources
Beta strandi396 – 3994Combined sources
Helixi407 – 42014Combined sources
Helixi424 – 4263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DTYX-ray2.14A/B1-429[»]
1MGVX-ray2.10A/B1-429[»]
1MLYX-ray1.81A/B1-429[»]
1MLZX-ray2.15A/B1-429[»]
1QJ3X-ray2.70A/B1-429[»]
1QJ5X-ray1.80A/B1-429[»]
1S06X-ray2.20A/B1-429[»]
1S07X-ray2.42A/B1-429[»]
1S08X-ray2.10A/B1-429[»]
1S09X-ray1.83A/B1-429[»]
1S0AX-ray1.71A/B1-429[»]
ProteinModelPortaliP12995.
SMRiP12995. Positions 1-429.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12995.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni112 – 1132Pyridoxal phosphate binding
Regioni308 – 3092Pyridoxal phosphate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0161.
HOGENOMiHOG000020209.
InParanoidiP12995.
KOiK00833.
OMAiPWQERRG.
OrthoDBiEOG6QVRHN.
PhylomeDBiP12995.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00834. BioA.
InterProiIPR005814. Aminotrans_3.
IPR005815. BioA.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00508. bioA. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12995-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTDDLAFDQ RHIWHPYTSM TSPLPVYPVV SAEGCELILS DGRRLVDGMS
60 70 80 90 100
SWWAAIHGYN HPQLNAAMKS QIDAMSHVMF GGITHAPAIE LCRKLVAMTP
110 120 130 140 150
QPLECVFLAD SGSVAVEVAM KMALQYWQAK GEARQRFLTF RNGYHGDTFG
160 170 180 190 200
AMSVCDPDNS MHSLWKGYLP ENLFAPAPQS RMDGEWDERD MVGFARLMAA
210 220 230 240 250
HRHEIAAVII EPIVQGAGGM RMYHPEWLKR IRKICDREGI LLIADEIATG
260 270 280 290 300
FGRTGKLFAC EHAEIAPDIL CLGKALTGGT MTLSATLTTR EVAETISNGE
310 320 330 340 350
AGCFMHGPTF MGNPLACAAA NASLAILESG DWQQQVADIE VQLREQLAPA
360 370 380 390 400
RDAEMVADVR VLGAIGVVET THPVNMAALQ KFFVEQGVWI RPFGKLIYLM
410 420
PPYIILPQQL QRLTAAVNRA VQDETFFCQ
Length:429
Mass (Da):47,336
Last modified:October 1, 1994 - v2
Checksum:i84D2D1AE3A1280FF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111R → P in CAA00964. 1 PublicationCurated
Sequence conflicti99 – 1024TPQP → SGRNA in AAA23514. (PubMed:3058702)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04423 Genomic DNA. Translation: AAA23514.1.
A11524 Unassigned DNA. Translation: CAA00964.1.
U00096 Genomic DNA. Translation: AAC73861.1.
AP009048 Genomic DNA. Translation: BAE76361.1.
PIRiF64813. XNECDP.
RefSeqiNP_415295.1. NC_000913.3.
YP_489047.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73861; AAC73861; b0774.
BAE76361; BAE76361; BAE76361.
GeneIDi12932847.
945376.
KEGGiecj:Y75_p0747.
eco:b0774.
PATRICi32116749. VBIEscCol129921_0800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04423 Genomic DNA. Translation: AAA23514.1 .
A11524 Unassigned DNA. Translation: CAA00964.1 .
U00096 Genomic DNA. Translation: AAC73861.1 .
AP009048 Genomic DNA. Translation: BAE76361.1 .
PIRi F64813. XNECDP.
RefSeqi NP_415295.1. NC_000913.3.
YP_489047.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P12995.
SMRi P12995. Positions 1-429.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9219N.
IntActi P12995. 5 interactions.
MINTi MINT-1275136.
STRINGi 511145.b0774.

Proteomic databases

PaxDbi P12995.
PRIDEi P12995.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73861 ; AAC73861 ; b0774 .
BAE76361 ; BAE76361 ; BAE76361 .
GeneIDi 12932847.
945376.
KEGGi ecj:Y75_p0747.
eco:b0774.
PATRICi 32116749. VBIEscCol129921_0800.

Organism-specific databases

EchoBASEi EB0115.
EcoGenei EG10117. bioA.

Phylogenomic databases

eggNOGi COG0161.
HOGENOMi HOG000020209.
InParanoidi P12995.
KOi K00833.
OMAi PWQERRG.
OrthoDBi EOG6QVRHN.
PhylomeDBi P12995.

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00160 .
BioCyci EcoCyc:DAPASYN-MONOMER.
ECOL316407:JW0757-MONOMER.
MetaCyc:DAPASYN-MONOMER.
BRENDAi 2.6.1.62. 2026.
SABIO-RK P12995.

Miscellaneous databases

EvolutionaryTracei P12995.
PROi P12995.

Gene expression databases

Genevestigatori P12995.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPi MF_00834. BioA.
InterProi IPR005814. Aminotrans_3.
IPR005815. BioA.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
PANTHERi PTHR11986. PTHR11986. 1 hit.
Pfami PF00202. Aminotran_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR00508. bioA. 1 hit.
PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Purification and properties of 7, 8-diaminopelargonic acid aminotransferase. An enzyme in the biotin biosynthetic pathway."
    Stoner G.L., Eisenberg M.A.
    J. Biol. Chem. 250:4029-4036(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN AMINOTRANSFERASE, SUBUNIT, SUBSTRATE SPECIFICITY, COFACTOR.
  6. "Biosynthesis of 7, 8-diaminopelargonic acid from 7-keto-8-aminopelargonic acid and S-adenosyl-L-methionine. The kinetics of the reaction."
    Stoner G.L., Eisenberg M.A.
    J. Biol. Chem. 250:4037-4043(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, ENZYME REGULATION.
  7. "Genetic and biochemical characterization of the birA gene and its product: evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli."
    Barker D.F., Campbell A.M.
    J. Mol. Biol. 146:469-492(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Inhibition of 7,8-diaminopelargonic acid aminotransferase by amiclenomycin and analogues."
    Mann S., Marquet A., Ploux O.
    Biochem. Soc. Trans. 33:802-805(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  9. "Biotin synthesis begins by hijacking the fatty acid synthetic pathway."
    Lin S., Hanson R.E., Cronan J.E.
    Nat. Chem. Biol. 6:682-688(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY.
  10. "Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes."
    Kaeck H., Sandmark J., Gibson K., Schneider G., Lindqvist Y.
    J. Mol. Biol. 291:857-876(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND PYRIDOXAL PHOSPHATE.
    Strain: B / BL21-DE3.
  11. "The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation."
    Eliot A.C., Sandmark J., Schneider G., Kirsch J.F.
    Biochemistry 41:12582-12589(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND MUTANTS ALA-391, MUTAGENESIS OF ARG-391, BIOPHYSICOCHEMICAL PROPERTIES.
  12. "Structural basis for the inhibition of the biosynthesis of biotin by the antibiotic amiclenomycin."
    Sandmark J., Mann S., Marquet A., Schneider G.
    J. Biol. Chem. 277:43352-43358(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, ENZYME REGULATION.
  13. "Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis."
    Sandmark J., Eliot A.C., Famm K., Schneider G., Kirsch J.F.
    Biochemistry 43:1213-1222(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS PHE-17; PHE-144; ASN-147; ALA-253 AND LYS-253 IN COMPLEX WITH PYRIDOXAL PHOSPHATE, MUTAGENESIS OF TYR-17; TYR-144; ASP-147 AND ARG-253.

Entry informationi

Entry nameiBIOA_ECOLI
AccessioniPrimary (citable) accession number: P12995
Secondary accession number(s): Q2MBJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 1, 1994
Last modified: November 26, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3