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B1HUT1 (GSA1_LYSSC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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 1

Short name=GSA 1
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1
Short name=GSA-AT 1
Gene names
Name:hemL1
Ordered Locus Names:Bsph_0332
OrganismLysinibacillus sphaericus (strain C3-41) [Complete proteome] [HAMAP]
Taxonomic identifier444177 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00375

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00375

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00375.

Sequence similarities

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

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete 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 – 429429Glutamate-1-semialdehyde 2,1-aminomutase 1 HAMAP-Rule MF_00375
PRO_0000382338

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B1HUT1 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 713570EA83CCA5BB

FASTA42945,738
        10         20         30         40         50         60 
MNHAKSEAVH AEALQHIVGG VNSPSRSYKA VGGGSPVAMV RGKGAYFWDV DGNRYIDYLA 

        70         80         90        100        110        120 
AYGPIVTGHG HPHIAKAITH AAENGTLFGT PTEYEVTFAN MLKEAIPSMD KVRFNNSGTE 

       130        140        150        160        170        180 
AVMTTIRVAR AYTGRTKIMK FAGCYHGHFD LVLVAAGSGP ATLGTPDSAG VTTSTAEEVI 

       190        200        210        220        230        240 
TVPFNNPEAF TEAMNTWGDE IAAILIEPIV GNFGIVEPNP GFLELVHATA KEKGALTIYD 

       250        260        270        280        290        300 
EVITAFRFHY GGAQNLLGLT PDLTALGKVI GGGLPIGAYG GRKEIMDTVA PLGPAYQAGT 

       310        320        330        340        350        360 
MAGNPASMQA GIACLEVLQT PGIYDEMDRL GGILEEGILA AAKEHGVTIT LNRLKGALTI 

       370        380        390        400        410        420 
YFTDVKVENY EQAENSNGEI FGRFFKLMLE QGVNLAPSKY EAWFLTTEHT EADILETIKA 


VNYAFSQLS 

« Hide

References

[1]"Complete genome sequence of the mosquitocidal bacterium Bacillus sphaericus C3-41 and comparison with those of closely related Bacillus species."
Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M., Berry C., Yuan Z.
J. Bacteriol. 190:2892-2902(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C3-41.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000817 Genomic DNA. Translation: ACA37961.1.
RefSeqYP_001696091.1. NC_010382.1.

3D structure databases

ProteinModelPortalB1HUT1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444177.Bsph_0332.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA37961; ACA37961; Bsph_0332.
GeneID6020830.
KEGGlsp:Bsph_0332.
PATRIC22413115. VBILysSph89750_0476.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAPVVMERA.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycLSPH444177:GJEL-345-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.
ProtoNetSearch...

Entry information

Entry nameGSA1_LYSSC
AccessionPrimary (citable) accession number: B1HUT1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: April 29, 2008
Last modified: May 14, 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