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Protein

Adenosylmethionine-8-amino-7-oxononanoate aminotransferase

Gene

bioA

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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.UniRule annotation1 Publication

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei18 – 181Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAMUniRule annotation
Binding sitei51 – 511SubstrateUniRule annotation
Binding sitei144 – 1441SubstrateUniRule annotation
Binding sitei243 – 2431Pyridoxal phosphateUniRule annotation
Binding sitei272 – 2721SubstrateUniRule annotation
Binding sitei306 – 3061Substrate; via carbonyl oxygenUniRule annotation
Binding sitei390 – 3901SubstrateUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. biotin biosynthetic process Source: UniProtKB-HAMAP
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

UniPathwayiUPA00078; UER00160.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosylmethionine-8-amino-7-oxononanoate aminotransferaseUniRule annotation (EC:2.6.1.62UniRule annotation)
Alternative name(s):
7,8-diamino-pelargonic acid aminotransferaseUniRule annotation
Short name:
DAPA ATUniRule annotation
Short name:
DAPA aminotransferaseUniRule annotation
7,8-diaminononanoate synthaseUniRule annotation
Short name:
DANSUniRule annotation
Diaminopelargonic acid synthaseUniRule annotation
Gene namesi
Name:bioAUniRule annotation
Ordered Locus Names:Cgl2604, cg2885
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000001009 Componenti: Chromosome UP000000582 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423Adenosylmethionine-8-amino-7-oxononanoate aminotransferasePRO_0000120365Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei272 – 2721N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi196627.cg2885.

Structurei

3D structure databases

ProteinModelPortaliP46395.
SMRiP46395. Positions 1-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 1122Pyridoxal phosphate bindingUniRule annotation
Regioni307 – 3082Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0161.
HOGENOMiHOG000020209.
KOiK00833.
OMAiYPWQERR.
OrthoDBiEOG6QVRHN.

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.

P46395-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENPSLRELD HRNIWHPYAA PGVRNRLVTK TDGVFLTLED GSTVIDAMSS
60 70 80 90 100
WWSAIHGHGH PRLKAAAQKQ IDTMSHVMFG GLTHEPAIKL THKLLNLTGN
110 120 130 140 150
SFDHVFYSDS GSVSVEVAIK MALQASKGQG HPERTKLLTW RSGYHGDTFT
160 170 180 190 200
AMSVCDPENG MHSLWKGTLP EQIFAPAPPV RGSSPQAISE YLRSMELLID
210 220 230 240 250
ETVSAIIIEP IVQGAGGMRF HDVALIEGVA TLCKKHDRFL IVDEIATGFG
260 270 280 290 300
RTGELFATLS NGLQPDIMCV GKALTGGFMS FAATLCTDKV AQLISTPNGG
310 320 330 340 350
GALMHGPTFM ANPLACAVSH ASLEIIETGM WQKQVKRIEA ELIAGLSPLQ
360 370 380 390 400
HLPGVADVRV LGAIGVIEME QNVNVEEATQ AALDHGVWIR PFGRLLYVMP
410 420
PYITTSEQCA QICTALHAAV KGK
Length:423
Mass (Da):45,741
Last modified:August 13, 2002 - v2
Checksum:i88773BED8418632D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301K → N in BAA03167 (PubMed:8161820).Curated
Sequence conflicti65 – 651A → R in BAA03167 (PubMed:8161820).Curated
Sequence conflicti101 – 1011S → A in BAA03167 (PubMed:8161820).Curated
Sequence conflicti193 – 1931R → H in BAA03167 (PubMed:8161820).Curated
Sequence conflicti231 – 2311T → A in BAA03167 (PubMed:8161820).Curated
Sequence conflicti263 – 2631L → V in BAA03167 (PubMed:8161820).Curated
Sequence conflicti285 – 2851L → V in BAA03167 (PubMed:8161820).Curated
Sequence conflicti295 – 2984STPN → RSPE in BAA03167 (PubMed:8161820).Curated
Sequence conflicti302 – 3021A → V in BAA03167 (PubMed:8161820).Curated
Sequence conflicti317 – 3171A → E in BAA03167 (PubMed:8161820).Curated
Sequence conflicti337 – 3371R → K in BAA03167 (PubMed:8161820).Curated
Sequence conflicti341 – 3411E → K in BAA03167 (PubMed:8161820).Curated
Sequence conflicti350 – 3523QHL → RCI in BAA03167 (PubMed:8161820).Curated
Sequence conflicti414 – 4141T → R in BAA03167 (PubMed:8161820).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14083 Genomic DNA. Translation: BAA03167.1.
BA000036 Genomic DNA. Translation: BAB99997.1.
BX927155 Genomic DNA. Translation: CAF21266.1.
PIRiI40336.
RefSeqiNP_601805.1. NC_003450.3.
YP_226845.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB99997; BAB99997; BAB99997.
GeneIDi1020551.
KEGGicgb:cg2885.
cgl:NCgl2515.
PATRICi21497254. VBICorGlu203724_2540.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14083 Genomic DNA. Translation: BAA03167.1.
BA000036 Genomic DNA. Translation: BAB99997.1.
BX927155 Genomic DNA. Translation: CAF21266.1.
PIRiI40336.
RefSeqiNP_601805.1. NC_003450.3.
YP_226845.1. NC_006958.1.

3D structure databases

ProteinModelPortaliP46395.
SMRiP46395. Positions 1-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg2885.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB99997; BAB99997; BAB99997.
GeneIDi1020551.
KEGGicgb:cg2885.
cgl:NCgl2515.
PATRICi21497254. VBICorGlu203724_2540.

Phylogenomic databases

eggNOGiCOG0161.
HOGENOMiHOG000020209.
KOiK00833.
OMAiYPWQERR.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00160.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic organization of the biotin biosynthetic genes of coryneform bacteria: cloning and sequencing of the bioA-bioD genes from Brevibacterium flavum."
    Hatakeyama K., Hohama K., Vertes A.A., Kobayashi M., Kurusu Y., Yukawa H.
    DNA Seq. 4:177-184(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: MJ233.
  2. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
    Ikeda M., Nakagawa S.
    Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Entry informationi

Entry nameiBIOA_CORGL
AccessioniPrimary (citable) accession number: P46395
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 13, 2002
Last modified: April 1, 2015
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.