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A2BL27 (GSA_HYPBU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. Feed History...

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

Names and origin

Protein namesRecommended name:
Glutamate-1-semialdehyde 2,1-aminomutase

Short name=GSA
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name=GSA-AT
Gene names
Name:hemL
Ordered Locus Names:Hbut_0837
OrganismHyperthermus butylicus (strain DSM 5456 / JCM 9403) [Reference proteome] [HAMAP]
Taxonomic identifier415426 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

transaminase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000059991

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A2BL27 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 7FD5942F85CE8581

FASTA42646,427
        10         20         30         40         50         60 
MPGEVSRSLY EKALTLFPGG VNSPVRAAVK PYPFYVERAE GPYIYTVDGE KLIDYVLAYG 

        70         80         90        100        110        120 
PLILGHKHPR VEEAVRRQLE KGWLYGAPYE LEIRLAEKIL KYYHPGGMVR FVNTGTEATM 

       130        140        150        160        170        180 
TAIRLARGVT GRKYIVKFNG CYHGAHDAVL VGAGSAAAEY GVPTSKGIPE EVAKLTLVAK 

       190        200        210        220        230        240 
YNDIESVEKI MSKHGDEVAA IIVEPVAGNA GVIPPKKGFL QELRRIASEH GALLIMDEVI 

       250        260        270        280        290        300 
TGFRLALGGA QEYYRVKADI TTLGKIVGGG FPIGVVVADR KIMEHLTPSG KVFNAGTFNA 

       310        320        330        340        350        360 
HPVTMAAGLA TIEVLEEGTP YRVASEAGRA LAEELESLVL SYGIDAAVNH VESMLQIFFV 

       370        380        390        400        410        420 
KGEVWSPEDA AKSDKKLYLK LHEELLKLGV FIAPSQMEAI FTSAAHTSDV VSETIEKLRK 


AFKRLR 

« Hide

References

[1]"The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5456 / JCM 9403.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000493 Genomic DNA. Translation: ABM80688.1.
RefSeqYP_001013033.1. NC_008818.1.

3D structure databases

ProteinModelPortalA2BL27.
SMRA2BL27. Positions 3-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING415426.Hbut_0837.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM80688; ABM80688; Hbut_0837.
GeneID4782262.
KEGGhbu:Hbut_0837.

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAPGFKPDI.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycHBUT415426:GC56-837-MONOMER.
UniPathwayUPA00251; UER00317.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_00375. HemL_aminotrans_3.
InterProIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00713. hemL. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_HYPBU
AccessionPrimary (citable) accession number: A2BL27
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 20, 2007
Last modified: February 19, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways