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Q5L2S4 (GSA1_GEOKA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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:GK0471
OrganismGeobacillus kaustophilus (strain HTA426) [Complete proteome] [HAMAP]
Taxonomic identifier235909 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length428 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 – 428428Glutamate-1-semialdehyde 2,1-aminomutase 1 HAMAP-Rule MF_00375
PRO_0000243573

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5L2S4 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 0EDA647DF671CD7A

FASTA42846,142
        10         20         30         40         50         60 
MQWTKSEQLY KEALQHIVGG VNSPSRSYKA VGGGAPVVME RAQGAYFWDV DGNKYIDYLA 

        70         80         90        100        110        120 
AYGPIIAGHA HPHIAEAIRR AAETGVLYGT PTPHEITFAK MLKEAIPSLE KVRFVNSGTE 

       130        140        150        160        170        180 
AVMTTIRVAR AYTGRSKIVK FEGCYHGHSD LVLVAAGSGP STLGTPDSAG VPPSIAQEVI 

       190        200        210        220        230        240 
TVPYNDVESF REAMNVWGEQ VAAVLVEPIV GNFGIVLPKP GFLEAINEIA HKEGALVIYD 

       250        260        270        280        290        300 
EVITAFRFMY GGAQNLLGVE PDLTAMGKII GGGLPIGAYG GRQDIMEQVA PLGPAYQAGT 

       310        320        330        340        350        360 
MAGNPASVLA GIACLEVLKQ EGVYEHLDRL GAMLEEGILA HARQCGLPVT VNRLKGALTV 

       370        380        390        400        410        420 
FFTDEKVENY KQAQRSDGEL FAKFFKLMLK QGINLAPSKY EAWFITLAHT EDDIAYTIDA 


VGKAFRQL 

« Hide

References

[1]"Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus."
Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.
Nucleic Acids Res. 32:6292-6303(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTA426.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000043 Genomic DNA. Translation: BAD74756.1.
RefSeqYP_146324.1. NC_006510.1.

3D structure databases

ProteinModelPortalQ5L2S4.
SMRQ5L2S4. Positions 1-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING235909.GK0471.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD74756; BAD74756; GK0471.
GeneID3184633.
KEGGgka:GK0471.
PATRIC21962111. VBIGeoKau81518_0551.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAPVVMERA.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycGKAU235909:GJO7-522-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 nameGSA1_GEOKA
AccessionPrimary (citable) accession number: Q5L2S4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 1, 2005
Last modified: May 14, 2014
This is version 68 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