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B2U6Q7 (GSA_RALPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:Rpic_0610
OrganismRalstonia pickettii (strain 12J) [Complete proteome] [HAMAP]
Taxonomic identifier402626 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

Protein attributes

Sequence length433 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 – 433433Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000121912

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2U6Q7 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 07E960D986BA61F7

FASTA43345,734
        10         20         30         40         50         60 
MSTPSRSAAL FERAQKTIPG GVNSPVRAFR SVGGIPRFIA KAAGPYLWDA DGTRYIDYVG 

        70         80         90        100        110        120 
SWGPMIVGHA HPEVVRAVQE VAADSFSFGA PTEAEVVMAE EICKLVPSIE QVRLVSSGTE 

       130        140        150        160        170        180 
ATMSALRLAR GFTGRDLIVK FEGCYHGHAD SLLVKAGSGL LTFADTTQNA PSSTGVPEDV 

       190        200        210        220        230        240 
VKHTMVLPYN DVAALREAFA RHGKEIAAVI VEPVAGNMNL VRGSNEFHQA MRALCTEHGA 

       250        260        270        280        290        300 
VLIFDEVMTG FRVALGCAQA LYGIKPDLTC LGKVIGGGMP AAAFGGRRDI MGFLAPLGSV 

       310        320        330        340        350        360 
YQAGTLSGNP LAVAAGLTTL RLIAAEGFHD RLATQTRKLV DGLAEIAREV GVPFAADSVG 

       370        380        390        400        410        420 
GMFGIYFREG VPTSFAEVTK SDVGRFNAFF HAMLDQGVYL APSAFEAGFV SSTHDDAILD 

       430 
ATFEAARKAF KAV 

« Hide

References

[1]"Complete sequence of chromosome 1 of Ralstonia pickettii 12J."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Marsh T., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 12J.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001068 Genomic DNA. Translation: ACD25761.1.
RefSeqYP_001898193.1. NC_010682.1.

3D structure databases

ProteinModelPortalB2U6Q7.
SMRB2U6Q7. Positions 1-429.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING402626.Rpic_0610.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD25761; ACD25761; Rpic_0610.
GeneID6287897.
KEGGrpi:Rpic_0610.
PATRIC20252096. VBIRalPic63053_1815.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACGHANER.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycRPIC402626:GH94-611-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_RALPJ
AccessionPrimary (citable) accession number: B2U6Q7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 45 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