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Q0SF42 (GSA_RHOSR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:RHA1_ro02037
OrganismRhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP]
Taxonomic identifier101510 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

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 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 – 441441Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000300942

Amino acid modifications

Modified residue2761N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0SF42 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: E12F16D68128273B

FASTA44145,450
        10         20         30         40         50         60 
MTVSSGDPDV HASRSAQLFE RADLVIPGGV NSPVRAFHSV GGTPRFIKEA SGYTLTDVDG 

        70         80         90        100        110        120 
NDYVDLICSW GPMILGHAHP AVVEAVQKAA ATGLSFGAPT EGEIELAEEI VGRVAPVEKV 

       130        140        150        160        170        180 
RLVNSGTEAT MSAVRLARGF TGRTKVLKFS GCYHGHVDAL LADAGSGLAT FGLPTSPGVT 

       190        200        210        220        230        240 
GAQAEDTIVV PYNDLDAVAQ AFAANEGRIA CVITEAAAGN MGAVAPQPGF NEGLRKLTSD 

       250        260        270        280        290        300 
NGALLIMDEV MTGFRVSSAG WFGLDGVAGD LYTFGKVMSG GLPAAAFGGR ADVMAHLAPA 

       310        320        330        340        350        360 
GPVYQAGTLS GNPVAVAAGL ASLRAADQGV YDALERNSAT LRTLLSDALT AESVPHRVQT 

       370        380        390        400        410        420 
AGTMLSVFFS EDPVTNYAEA KAAQTWRFPA FFHGLLSRGV YPPPSAFEAW FVSAAMDDRA 

       430        440 
FSIIADALPH AAKAAAAAVQ P 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000431 Genomic DNA. Translation: ABG93844.1.
RefSeqYP_702002.1. NC_008268.1.

3D structure databases

ProteinModelPortalQ0SF42.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING101510.RHA1_ro02037.

Proteomic databases

PRIDEQ0SF42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG93844; ABG93844; RHA1_ro02037.
GeneID4218083.
KEGGrha:RHA1_ro02037.
PATRIC23202919. VBIRhoJos26306_2061.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycRJOS101510:GJJ1-2035-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_RHOSR
AccessionPrimary (citable) accession number: Q0SF42
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 5, 2006
Last modified: February 19, 2014
This is version 57 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