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Q9ZEU7 (ECTB_CHRSD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Diaminobutyrate--2-oxoglutarate transaminase

EC=2.6.1.76
Alternative name(s):
DABA aminotransferase
Diaminobutyrate--2-oxoglutarate aminotransferase
L-2,4-diaminobutyric acid transaminase
Gene names
Name:ectB
Ordered Locus Names:Csal_1877
OrganismChromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]
Taxonomic identifier290398 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHalomonadaceaeChromohalobacter

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes reversively the conversion of L-aspartate beta-semialdehyde (ASA) to L-2,4-diaminobutyrate (DABA) by transamination with L-glutamate By similarity.

Catalytic activity

L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde + L-glutamate.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 1/3.

Subunit structure

Homohexamer By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 423423Diaminobutyrate--2-oxoglutarate transaminase
PRO_0000120522

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q9ZEU7 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 735C6BCF5A88288C

FASTA42346,200
        10         20         30         40         50         60 
MQTQILERME SEVRTYSRSF PTVFTEAKGA RLHAEDGNQY IDFLAGAGTL NYGHNHPKLK 

        70         80         90        100        110        120 
QALADYIASD GIVHGLDMWS AAKRDYLETL EEVILKPRGL DYKVHLPGPT GTNAVEAAIR 

       130        140        150        160        170        180 
LARNAKGRHN IVTFTNGFHG VTMGALATTG NRKFREATGG IPTQGASFMP FDGYMGEGVD 

       190        200        210        220        230        240 
TLSYFEKLLG DNSGGLDVPA AVIIETVQGE GGINPAGIPW LQRLEKICRD HDMLLIVDDI 

       250        260        270        280        290        300 
QAGCGRTGKF FSFEHAGITP DIVTNSKSLS GFGLPFAHVL MRPELDIWKP GQYNGTFRGF 

       310        320        330        340        350        360 
NLAFVTAAAA MRHFWSDDTF ERDVQRKGRV VEDRFQKLAS FMTEKGHPAS ERGRGLMRGL 

       370        380        390        400        410        420 
DVGDGDMADK ITAQAFKNGL IIETSGHSGQ VIKCLCPLTI TDEDLVGGLD ILEQSVKEVF 


GQA 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the genes for the biosynthesis of the compatible solute ectoine in the moderately halophilic bacterium Halomonas elongata DSM 3043."
Canovas D., Vargas C., Calderon M.I., Ventosa A., Nieto J.J.
Syst. Appl. Microbiol. 21:487-497(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Chromohalobacter salexigens DSM 3043."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., Canovas D., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 3043 / ATCC BAA-138 / NCIMB 13768.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ011103 Genomic DNA. Translation: CAA09484.1.
CP000285 Genomic DNA. Translation: ABE59229.1.
RefSeqYP_573928.1. NC_007963.1.

3D structure databases

ProteinModelPortalQ9ZEU7.
ModBaseSearch...

Protein-protein interaction databases

STRING290398.Csal_1877.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE59229; ABE59229; Csal_1877.
GeneID4028240.
KEGGcsa:Csal_1877.
PATRIC21447566. VBIChrSal113723_1889.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0160.
HOGENOMHOG000020206.
KOK00836.
OMAYSRGWPV.
ProtClustDBPRK09264.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-801.
UniPathwayUPA00067; UER00121.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProIPR005814. Aminotrans_3.
IPR004637. Dat.
IPR012773. Ectoine_EctB.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF7. PTHR11986:SF7. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00709. dat. 1 hit.
TIGR02407. ectoine_ectB. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameECTB_CHRSD
AccessionPrimary (citable) accession number: Q9ZEU7
Secondary accession number(s): Q1QWC9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 1, 2013
This is version 85 of the entry and version 1 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