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Protein

Adenosylmethionine-8-amino-7-oxononanoate aminotransferase

Gene

bioA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

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
  1. Vmax=0.16 µmol/min/mg enzyme with KAPA as substrate2 Publications
  2. Vmax=0.027 µmol/min/mg enzyme with 8-keto-7-aminopelargonic acid as substrate2 Publications

Pathwayi: biotin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route).
Proteins known to be involved in this subpathway in this organism are:
  1. Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (bioA)
This subpathway is part of the pathway biotin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route), the pathway biotin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei17Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAMCurated1
Binding sitei52Substrate1 Publication1
Binding sitei144Substrate1 Publication1
Binding sitei245Pyridoxal phosphate3 Publications1
Binding sitei274Substrate1 Publication1
Binding sitei307Substrate; via carbonyl oxygen1 Publication1
Binding sitei391Substrate1 Publication1

GO - Molecular functioni

  • adenosylmethionine-8-amino-7-oxononanoate transaminase activity Source: UniProtKB
  • pyridoxal phosphate binding Source: UniProtKB

GO - Biological processi

  • biotin biosynthetic process Source: UniProtKB

Keywordsi

Molecular functionAminotransferase, Transferase
Biological processBiotin biosynthesis
LigandPyridoxal phosphate, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciEcoCyc:DAPASYN-MONOMER
MetaCyc:DAPASYN-MONOMER
BRENDAi2.6.1.62 2026
SABIO-RKiP12995
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10117 bioA

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi17Y → F: Severely reduces the aminotransferase activity. 1 Publication1
Mutagenesisi144Y → F: Severely reduces the aminotransferase activity. 1 Publication1
Mutagenesisi147D → N: Loss of aminotransferase activity. 1 Publication1
Mutagenesisi253R → A: Has only a small effect on the rate of reaction with DAPA. 1 Publication1
Mutagenesisi253R → K: Increases aminotransferase activity toward SAM. 1 Publication1
Mutagenesisi253R → M: Loss of aminotransferase activity. 1 Publication1
Mutagenesisi253R → Q: Increases aminotransferase activity toward SAM. 1 Publication1
Mutagenesisi391R → A: Reduces aminotransferase activity. 1 Publication1

Chemistry databases

DrugBankiDB02274 7-Keto-8-Aminopelargonic Acid
DB04083 N'-Pyridoxyl-Lysine-5'-Monophosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001203661 – 429Adenosylmethionine-8-amino-7-oxononanoate aminotransferaseAdd BLAST429

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei274N6-(pyridoxal phosphate)lysine1

Proteomic databases

PaxDbiP12995
PRIDEiP12995

Expressioni

Inductioni

Repressed by BirA.1 Publication

Interactioni

Subunit structurei

Homodimer.5 Publications

Protein-protein interaction databases

BioGridi4261841, 13 interactors
DIPiDIP-9219N
IntActiP12995, 5 interactors
STRINGi316385.ECDH10B_0842

Structurei

Secondary structure

1429
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 12Combined sources10
Beta strandi20 – 22Combined sources3
Beta strandi27 – 34Combined sources8
Beta strandi36 – 39Combined sources4
Beta strandi44 – 49Combined sources6
Turni50 – 54Combined sources5
Helixi62 – 74Combined sources13
Beta strandi81 – 84Combined sources4
Helixi86 – 98Combined sources13
Beta strandi105 – 111Combined sources7
Helixi112 – 130Combined sources19
Beta strandi136 – 140Combined sources5
Helixi149 – 152Combined sources4
Turni157 – 161Combined sources5
Helixi162 – 165Combined sources4
Turni166 – 168Combined sources3
Beta strandi173 – 175Combined sources3
Beta strandi180 – 184Combined sources5
Helixi188 – 191Combined sources4
Helixi192 – 201Combined sources10
Turni202 – 204Combined sources3
Beta strandi205 – 210Combined sources6
Beta strandi212 – 215Combined sources4
Turni217 – 219Combined sources3
Beta strandi221 – 223Combined sources3
Helixi226 – 238Combined sources13
Beta strandi241 – 245Combined sources5
Turni247 – 254Combined sources8
Beta strandi255 – 258Combined sources4
Helixi259 – 263Combined sources5
Beta strandi268 – 272Combined sources5
Helixi274 – 277Combined sources4
Beta strandi278 – 281Combined sources4
Beta strandi284 – 288Combined sources5
Helixi290 – 297Combined sources8
Beta strandi299 – 303Combined sources5
Turni309 – 312Combined sources4
Helixi314 – 328Combined sources15
Helixi332 – 347Combined sources16
Helixi348 – 352Combined sources5
Beta strandi356 – 362Combined sources7
Beta strandi365 – 372Combined sources8
Helixi376 – 385Combined sources10
Beta strandi396 – 399Combined sources4
Helixi407 – 420Combined sources14
Helixi424 – 426Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12995

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni112 – 113Pyridoxal phosphate binding2
Regioni308 – 309Pyridoxal phosphate binding2

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108JPX Bacteria
COG0161 LUCA
HOGENOMiHOG000020209
InParanoidiP12995
KOiK00833
OMAiGVWLEDF
PhylomeDBiP12995

Family and domain databases

CDDicd00610 OAT_like, 1 hit
Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_00834 BioA, 1 hit
InterProiView protein in InterPro
IPR005814 Aminotrans_3
IPR005815 BioA
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00202 Aminotran_3, 1 hit
PIRSFiPIRSF000521 Transaminase_4ab_Lys_Orn, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR00508 bioA, 1 hit
PROSITEiView protein in PROSITE
PS00600 AA_TRANSFER_CLASS_3, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti11R → P in CAA00964 (Ref. 2) Curated1
Sequence conflicti99 – 102TPQP → SGRNA in AAA23514 (PubMed:3058702).Curated4

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
WP_001295303.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73861; AAC73861; b0774
BAE76361; BAE76361; BAE76361
GeneIDi945376
KEGGiecj:JW0757
eco:b0774
PATRICifig|511145.12.peg.800

Similar proteinsi

Entry informationi

Entry nameiBIOA_ECOLI
AccessioniPrimary (citable) accession number: P12995
Secondary accession number(s): Q2MBJ5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 1, 1994
Last modified: March 28, 2018
This is version 161 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health