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C0ZUX9 (GSA_RHOE4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:RER_16660
OrganismRhodococcus erythropolis (strain PR4 / NBRC 100887) [Complete proteome] [HAMAP]
Taxonomic identifier234621 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length432 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 – 432432Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382363

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C0ZUX9 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 3579AB5654B42FF9

FASTA43244,563
        10         20         30         40         50         60 
MHATNSARLF ERAGNVIPGG VNSPVRAFGS VGGTPRFIRE ASGYTLTDVD GNNYVDLVSS 

        70         80         90        100        110        120 
WGPMILGHAH PAVVEAVREA ALGGLSFGAP TEGEVALAEE IVARVAPVEK VRLVNSGTEA 

       130        140        150        160        170        180 
TMSAVRLARG FTGRTKIIKF SGCYHGHVDA LLADAGSGLA TFGLPTSPGV TGAQAEDTIV 

       190        200        210        220        230        240 
VRYNDLDAVA AAFAANPGAI ACVITEAAAG NMGAVAPLPG FNEGLRRLTR EHGALLIMDE 

       250        260        270        280        290        300 
VMTGFRVSAS GWYGIDNVAG DLYTFGKVMS GGLPAAAFGG RADIMGHLAP DGPVYQAGTL 

       310        320        330        340        350        360 
SGNPVAVAAG LASLRAADAE VYAKLGRNAT ALGDLMTQAL TAEGVEHRVQ YAGTLVSVFF 

       370        380        390        400        410        420 
TENTVTNYDE AKAAQTWRFP AFFHALLSRG VYPPPSAFEA WFVSAALDDR AFSIIADAMP 

       430 
HAAKAAAAAV KP 

« Hide

References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PR4 / NBRC 100887.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008957 Genomic DNA. Translation: BAH32374.1.
RefSeqYP_002765113.1. NC_012490.1.

3D structure databases

ProteinModelPortalC0ZUX9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234621.RER_16660.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH32374; BAH32374; RER_16660.
GeneID7715132.
KEGGrer:RER_16660.
PATRIC23189702. VBIRhoEry66701_2152.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycRERY234621:GHDE-1685-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_RHOE4
AccessionPrimary (citable) accession number: C0ZUX9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 26, 2009
Last modified: May 14, 2014
This is version 39 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