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Q06774 (GSA_PROFF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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
OrganismPropionibacterium freudenreichii subsp. freudenreichii
Taxonomic identifier66712 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length441 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.

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
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 – 441441Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120432

Amino acid modifications

Modified residue2701N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q06774 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 0F07395A67CAE4D2

FASTA44145,932
        10         20         30         40         50         60 
MSVSDELFAE ALKVMPGGVS SPVRAYRSVG GTPRFVKRAL GSHIVDVDDK RYVDLVCSWG 

        70         80         90        100        110        120 
PMIAGHAHPE VVAAVLQAVA DSTSFGAPSE VELRLAQAVV ARMGGAIDKV RFTCSGTEAV 

       130        140        150        160        170        180 
MTAARLARGI TKRPLLVKFV GCYHGHSDSF LVSAGSGVAS LGLPDSPGVP KEVAGDTVAL 

       190        200        210        220        230        240 
PYGRIDMVEE LFAERGDQVA AIVTEGVPAN MGVIVPPEGF NRRLHDIAHA HGALLIQDEV 

       250        260        270        280        290        300 
LTGFRLSPTG AWGLQGAKEG WTPDLFTFGK VIGGGMPLAA VGGSAQLMDY LAPEGPVYQA 

       310        320        330        340        350        360 
GTLSGNPAAC AAGLATLALM DDAAYSRLDA TADRVSAMAD AALESAGVPH RINKVSNLFS 

       370        380        390        400        410        420 
VFLTDAPVTD FASASKQDTK AFSRFFHAAL DAGLWLAPSG FEAWFCSTAL DDDDLEVIDA 

       430        440 
GLHKAAQAAA QGLSSLEDVR R 

« Hide

References

[1]"Cloning and characterization of the gene encoding glutamate 1-semialdehyde 2,1-aminomutase, which is involved in delta-aminolevulinic acid synthesis in Propionibacterium freudenreichii."
Murakami K., Hashimoto Y., Murooka Y.
Appl. Environ. Microbiol. 59:347-350(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 6207 / DSM 20271 / LMG 16412 / NBRC 12424 / NCIMB 5959 / NCTC 10470 / NRRL B-3523.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D12643 Genomic DNA. Translation: BAA02164.1.
D85417 Genomic DNA. Translation: BAA21914.1.
PIRA48959.

3D structure databases

ProteinModelPortalQ06774.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_PROFF
AccessionPrimary (citable) accession number: Q06774
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 19, 2014
This is version 83 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