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P46395 (BIOA_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:bioA
Ordered Locus Names:Cgl2604, cg2885
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium ›

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate. HAMAP-Rule MF_00834

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1. HAMAP-Rule MF_00834

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processBiotin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
S-adenosyl-L-methionine
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbiotin biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionadenosylmethionine-8-amino-7-oxononanoate transaminase activity

Inferred from electronic annotation. Source: HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 423423Adenosylmethionine-8-amino-7-oxononanoate aminotransferase HAMAP-Rule MF_00834
PRO_0000120365

Regions

Region111 – 1122Pyridoxal phosphate binding By similarity
Region307 – 3082Pyridoxal phosphate binding By similarity

Sites

Binding site511Substrate By similarity
Binding site1441Substrate By similarity
Binding site2431Pyridoxal phosphate By similarity
Binding site2721Substrate By similarity
Binding site3061Substrate; via carbonyl oxygen By similarity
Binding site3901Substrate By similarity
Site181Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM By similarity

Amino acid modifications

Modified residue2721N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict301K → N in BAA03167. Ref.1
Sequence conflict651A → R in BAA03167. Ref.1
Sequence conflict1011S → A in BAA03167. Ref.1
Sequence conflict1931R → H in BAA03167. Ref.1
Sequence conflict2311T → A in BAA03167. Ref.1
Sequence conflict2631L → V in BAA03167. Ref.1
Sequence conflict2851L → V in BAA03167. Ref.1
Sequence conflict295 – 2984STPN → RSPE in BAA03167. Ref.1
Sequence conflict3021A → V in BAA03167. Ref.1
Sequence conflict3171A → E in BAA03167. Ref.1
Sequence conflict3371R → K in BAA03167. Ref.1
Sequence conflict3411E → K in BAA03167. Ref.1
Sequence conflict350 – 3523QHL → RCI in BAA03167. Ref.1
Sequence conflict4141T → R in BAA03167. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P46395 [UniParc].

Last modified August 13, 2002. Version 2.
Checksum: 88773BED8418632D

FASTA42345,741
        10         20         30         40         50         60 
MENPSLRELD HRNIWHPYAA PGVRNRLVTK TDGVFLTLED GSTVIDAMSS WWSAIHGHGH 

        70         80         90        100        110        120 
PRLKAAAQKQ IDTMSHVMFG GLTHEPAIKL THKLLNLTGN SFDHVFYSDS GSVSVEVAIK 

       130        140        150        160        170        180 
MALQASKGQG HPERTKLLTW RSGYHGDTFT AMSVCDPENG MHSLWKGTLP EQIFAPAPPV 

       190        200        210        220        230        240 
RGSSPQAISE YLRSMELLID ETVSAIIIEP IVQGAGGMRF HDVALIEGVA TLCKKHDRFL 

       250        260        270        280        290        300 
IVDEIATGFG RTGELFATLS NGLQPDIMCV GKALTGGFMS FAATLCTDKV AQLISTPNGG 

       310        320        330        340        350        360 
GALMHGPTFM ANPLACAVSH ASLEIIETGM WQKQVKRIEA ELIAGLSPLQ HLPGVADVRV 

       370        380        390        400        410        420 
LGAIGVIEME QNVNVEEATQ AALDHGVWIR PFGRLLYVMP PYITTSEQCA QICTALHAAV 


KGK

« Hide

References

« Hide 'large scale' references
[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]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D14083 Genomic DNA. Translation: BAA03167.1.
BA000036 Genomic DNA. Translation: BAB99997.1.
BX927155 Genomic DNA. Translation: CAF21266.1.
PIRI40336.
RefSeqNP_601805.1. NC_003450.3.
YP_226845.1. NC_006958.1.

3D structure databases

ProteinModelPortalP46395.
SMRP46395. Positions 1-421.
ModBaseSearch...

Protein-protein interaction databases

STRING196627.cg2885.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB99997; BAB99997; BAB99997.
CAF21266; CAF21266; cg2885.
GeneID1020551.
3342736.
KEGGcgb:cg2885.
cgl:NCgl2515.
PATRIC21497254. VBICorGlu203724_2540.

Phylogenomic databases

eggNOGCOG0161.
HOGENOMHOG000020209.
KOK00833.
OMAHASLEII.
ProtClustDBPRK05630.

Enzyme and pathway databases

BioCycCGLU196627:GJDM-2593-MONOMER.
UniPathwayUPA00078; UER00160.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_00834. BioA.
InterProIPR005814. Aminotrans_3.
IPR005815. BioA.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF8. PTHR11986:SF8. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00508. bioA. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBIOA_CORGL
AccessionPrimary (citable) accession number: P46395
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 13, 2002
Last modified: May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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