UniProtKB - P9WQ81 (BIOA_MYCTU)
Protein
Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
Gene
bioA
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Catalyzes the reversible 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. Can also use sinefungin as substrate.1 Publication
Miscellaneous
Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism.
Catalytic activityi
- 8-amino-7-oxononanoate + S-adenosyl-L-methionine = 7,8-diaminononanoate + S-adenosyl-4-methylsulfanyl-2-oxobutanoateEC:2.6.1.62
Cofactori
pyridoxal 5'-phosphate1 Publication
Activity regulationi
Competitively inhibited by KAPA at concentrations above 10 µM and amiclenomycin.1 Publication
Kineticsi
- KM=3.8 µM for KAPA (at pH 8.6 and at 37 degrees Celsius)2 Publications
- KM=450 µM for SAM (at pH 8.6 and at 37 degrees Celsius)2 Publications
- KM=700 µM for sinefungin (at pH 8.6 and at 37 degrees Celsius)2 Publications
- Vmax=22 µmol/min/mg enzyme (at pH 8.6 and at 37 degrees Celsius)2 Publications
: biotin biosynthesis Pathwayi
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:
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (bioA)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 25 | Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM | 1 | |
Binding sitei | 64 | SubstrateBy similarity | 1 | |
Binding sitei | 157 | Substrate1 Publication | 1 | |
Binding sitei | 254 | Pyridoxal phosphateBy similarity | 1 | |
Binding sitei | 283 | SubstrateBy similarity | 1 | |
Binding sitei | 316 | Substrate; via carbonyl oxygen1 Publication | 1 | |
Binding sitei | 400 | Substrate1 Publication | 1 |
GO - Molecular functioni
- adenosylmethionine-8-amino-7-oxononanoate transaminase activity Source: MTBBASE
- pyridoxal phosphate binding Source: UniProtKB-UniRule
GO - Biological processi
- biotin biosynthetic process Source: MTBBASE
Keywordsi
Molecular function | Aminotransferase, Transferase |
Biological process | Biotin biosynthesis |
Ligand | Pyridoxal phosphate, S-adenosyl-L-methionine |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-5756-MONOMER |
BRENDAi | 2.6.1.62 3445 |
UniPathwayi | UPA00078;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:Rv1568 ORF Names:MTCY336.35c |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv1568 |
Subcellular locationi
- Cytoplasm By similarity
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 25 | Y → A: Does not show detectable activity at 335 nm with SAM, even up to concentrations of 3 mM, and shows approximately 70% reduced activity with high concentrations of DAPA (0.5 mM). 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL2146299 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000120374 | 1 – 437 | Adenosylmethionine-8-amino-7-oxononanoate aminotransferaseAdd BLAST | 437 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 283 | N6-(pyridoxal phosphate)lysine | 1 |
Proteomic databases
PaxDbi | P9WQ81 |
Interactioni
Subunit structurei
Homodimer.
2 PublicationsProtein-protein interaction databases
STRINGi | 83332.Rv1568 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P9WQ81 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 124 – 125 | Pyridoxal phosphate binding | 2 | |
Regioni | 317 – 318 | Pyridoxal phosphate binding | 2 |
Sequence similaritiesi
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.Curated
Phylogenomic databases
eggNOGi | ENOG4108JPX Bacteria COG0161 LUCA |
KOi | K00833 |
OMAi | GVWLEDF |
PhylomeDBi | P9WQ81 |
Family and domain databases
CDDi | cd00610 OAT_like, 1 hit |
Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 1 hit |
HAMAPi | MF_00834 BioA, 1 hit |
InterProi | View protein in InterPro IPR005814 Aminotrans_3 IPR005815 BioA IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major |
Pfami | View protein in Pfam PF00202 Aminotran_3, 1 hit |
SUPFAMi | SSF53383 SSF53383, 1 hit |
TIGRFAMsi | TIGR00508 bioA, 1 hit |
PROSITEi | View protein in PROSITE PS00600 AA_TRANSFER_CLASS_3, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WQ81-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAAATGGLTP EQIIAVDGAH LWHPYSSIGR EAVSPVVAVA AHGAWLTLIR
60 70 80 90 100
DGQPIEVLDA MSSWWTAIHG HGHPALDQAL TTQLRVMNHV MFGGLTHEPA
110 120 130 140 150
ARLAKLLVDI TPAGLDTVFF SDSGSVSVEV AAKMALQYWR GRGLPGKRRL
160 170 180 190 200
MTWRGGYHGD TFLAMSICDP HGGMHSLWTD VLAAQVFAPQ VPRDYDPAYS
210 220 230 240 250
AAFEAQLAQH AGELAAVVVE PVVQGAGGMR FHDPRYLHDL RDICRRYEVL
260 270 280 290 300
LIFDEIATGF GRTGALFAAD HAGVSPDIMC VGKALTGGYL SLAATLCTAD
310 320 330 340 350
VAHTISAGAA GALMHGPTFM ANPLACAVSV ASVELLLGQD WRTRITELAA
360 370 380 390 400
GLTAGLDTAR ALPAVTDVRV CGAIGVIECD RPVDLAVATP AALDRGVWLR
410 420 430
PFRNLVYAMP PYICTPAEIT QITSAMVEVA RLVGSLP
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44332.1 |
PIRi | B70540 |
RefSeqi | NP_216084.1, NC_000962.3 WP_003407803.1, NZ_NVQJ01000004.1 |
Genome annotation databases
EnsemblBacteriai | CCP44332; CCP44332; Rv1568 |
GeneIDi | 886343 |
KEGGi | mtu:Rv1568 mtv:RVBD_1568 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44332.1 |
PIRi | B70540 |
RefSeqi | NP_216084.1, NC_000962.3 WP_003407803.1, NZ_NVQJ01000004.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3BV0 | X-ray | 2.21 | A/B | 1-437 | [»] | |
3LV2 | X-ray | 2.18 | A/B | 1-437 | [»] | |
3TFT | X-ray | 1.95 | A/B | 1-437 | [»] | |
3TFU | X-ray | 1.94 | A/B | 1-437 | [»] | |
4CXQ | X-ray | 1.80 | A/B | 1-437 | [»] | |
4CXR | X-ray | 1.70 | A/B | 1-437 | [»] | |
4MQP | X-ray | 1.83 | A/B | 1-437 | [»] | |
4MQQ | X-ray | 1.70 | A/B | 1-437 | [»] | |
4MQR | X-ray | 2.10 | A/B | 1-437 | [»] | |
4W1V | X-ray | 2.24 | A/B | 7-435 | [»] | |
4W1W | X-ray | 1.90 | A/B | 8-436 | [»] | |
4W1X | X-ray | 1.80 | A/B | 1-437 | [»] | |
4WYA | X-ray | 2.50 | A/B/C/D | 1-437 | [»] | |
4WYC | X-ray | 1.70 | A/B | 7-437 | [»] | |
4WYD | X-ray | 1.35 | A/B | 1-437 | [»] | |
4WYE | X-ray | 1.75 | A/B | 1-437 | [»] | |
4WYF | X-ray | 2.25 | A/B | 1-437 | [»] | |
4WYG | X-ray | 1.62 | A/B | 1-437 | [»] | |
4XEW | X-ray | 2.47 | A/B | 1-437 | [»] | |
4XJL | X-ray | 1.85 | A/B | 1-437 | [»] | |
4XJM | X-ray | 1.60 | A/B | 1-437 | [»] | |
4XJO | X-ray | 1.50 | A/B | 1-437 | [»] | |
4XJP | X-ray | 1.60 | A/B | 1-437 | [»] | |
SMRi | P9WQ81 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv1568 |
Chemistry databases
ChEMBLi | CHEMBL2146299 |
Proteomic databases
PaxDbi | P9WQ81 |
Genome annotation databases
EnsemblBacteriai | CCP44332; CCP44332; Rv1568 |
GeneIDi | 886343 |
KEGGi | mtu:Rv1568 mtv:RVBD_1568 |
Organism-specific databases
TubercuListi | Rv1568 |
Phylogenomic databases
eggNOGi | ENOG4108JPX Bacteria COG0161 LUCA |
KOi | K00833 |
OMAi | GVWLEDF |
PhylomeDBi | P9WQ81 |
Enzyme and pathway databases
UniPathwayi | UPA00078;UER00160 |
BioCyci | MTBH37RV:G185E-5756-MONOMER |
BRENDAi | 2.6.1.62 3445 |
Family and domain databases
CDDi | cd00610 OAT_like, 1 hit |
Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 1 hit |
HAMAPi | MF_00834 BioA, 1 hit |
InterProi | View protein in InterPro IPR005814 Aminotrans_3 IPR005815 BioA IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major |
Pfami | View protein in Pfam PF00202 Aminotran_3, 1 hit |
SUPFAMi | SSF53383 SSF53383, 1 hit |
TIGRFAMsi | TIGR00508 bioA, 1 hit |
PROSITEi | View protein in PROSITE PS00600 AA_TRANSFER_CLASS_3, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | BIOA_MYCTU | |
Accessioni | P9WQ81Primary (citable) accession number: P9WQ81 Secondary accession number(s): L0T781, O06622, P0A4X6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | October 16, 2019 | |
This is version 38 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references