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C0QCR9 (GSA_DESAH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:HRM2_20470
OrganismDesulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2) [Complete proteome] [HAMAP]
Taxonomic identifier177437 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfobacterium

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 HAMAP-Rule MF_00375
PRO_0000382308

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C0QCR9 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 723DA4502903177C

FASTA42844,666
        10         20         30         40         50         60 
METTRSEALF KEAAKFIPGG VNSPVRACGS VGGSPLFIQK AEGSKIIDAD GNVYIDYVGS 

        70         80         90        100        110        120 
WGPMILGHRH PDVVKALIEA LASGTSFGAP TALETRLSQL VVEAVPSVEK VRMVNSGTEA 

       130        140        150        160        170        180 
TMSAVRLARG YTGRDIIIKF DGGYHGHADT LLVAAGSGVA TLNIPGSPGI PESVSAHTLS 

       190        200        210        220        230        240 
ITYNDGEAVK RVMAEKGDRV AAIIVEPVAG NMGMVPPVKG FHETLRTLCT KHGALLIFDE 

       250        260        270        280        290        300 
VMTGFRVAKG SGQGLFGITP DLTCFGKIIG GGLPVGAYGG RREIMDQIAP AGPVYQAGTL 

       310        320        330        340        350        360 
SGNPLAMAAG IATLEALKKT GFYESLDAKT ERLVTGLRTA AEKAGIDFTA SHVGSMAGMF 

       370        380        390        400        410        420 
FTRATVTNFD EAKTSDLVNF SKFYTGMRDR GIYLAPSQFE ALFVSAAHTN DEIDATIAAA 


ADVMAGLV 

« Hide

References

[1]"Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate reducer oxidizing organic carbon completely to carbon dioxide."
Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S., Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A., Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O., Meyerdierks A., Gottschalk G., Amann R.
Environ. Microbiol. 11:1038-1055(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43914 / DSM 3382 / HRM2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001087 Genomic DNA. Translation: ACN15146.1.
RefSeqYP_002603310.1. NC_012108.1.

3D structure databases

ProteinModelPortalC0QCR9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING177437.HRM2_20470.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACN15146; ACN15146; HRM2_20470.
GeneID7502131.
KEGGdat:HRM2_20470.
PATRIC21683745. VBIDesAut25181_2141.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAFFERAST.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycDAUT177437:GHLR-2046-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_DESAH
AccessionPrimary (citable) accession number: C0QCR9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 5, 2009
Last modified: May 14, 2014
This is version 40 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