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Q5KWK9 (GSA2_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 2

Short name=GSA 2
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 2
Short name=GSA-AT 2
Gene names
Name:hemL2
Ordered Locus Names:GK2642
OrganismGeobacillus kaustophilus (strain HTA426) [Complete proteome] [HAMAP]
Taxonomic identifier235909 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

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 2 HAMAP-Rule MF_00375
PRO_0000243574

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5KWK9 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 80801747A6F78924

FASTA42946,530
        10         20         30         40         50         60 
MRSYERSKTA YEEAVKLMPG GVNSPVRAFK SVGMTPIFMA RGQGAKIYDI DGNEYIDYVL 

        70         80         90        100        110        120 
SWGPLILGHA NPQVVEALKR VAEQGTSFGA PTLLENELAK LVIERVPSVE IVRMVNSGTE 

       130        140        150        160        170        180 
ATMSALRLAR GYTKRNKIMK FEGSYHGHGD SLLIKAGSGV ATLGLPDSPG VPESVAQHTI 

       190        200        210        220        230        240 
TVPYNDLDSV RYAFERFGED IAAVIVEPVA GNMGVVPPVP GFLEGLREVT KQYGALLIFD 

       250        260        270        280        290        300 
EVMTGFRVDY HCAQGYYGIE PDLTCLGKVI GGGLPVGAYG GKAEIMELVA PSGPVYQAGT 

       310        320        330        340        350        360 
LSGNPLAMTA GYETLRQLTP ETYEELGRKA ARLADGLHQA AEKYDIPHTI NRAGSMIGFF 

       370        380        390        400        410        420 
FTNEPVVNYE TAKTSDLELF AAYYREMANE GIFLPPSQFE GLFLSTAHSD DDIEYTIAAA 


ERVFARLRG 

« 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: BAD76927.1.
RefSeqYP_148495.1. NC_006510.1.

3D structure databases

ProteinModelPortalQ5KWK9.
SMRQ5KWK9. Positions 5-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING235909.GK2642.

Proteomic databases

PRIDEQ5KWK9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD76927; BAD76927; GK2642.
GeneID3186832.
KEGGgka:GK2642.
PATRIC21966749. VBIGeoKau81518_2823.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycGKAU235909:GJO7-2737-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 nameGSA2_GEOKA
AccessionPrimary (citable) accession number: Q5KWK9
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