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Q5WWG1 (GSA_LEGPL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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:lpl1492
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length429 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 – 429429Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243580

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WWG1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 348F41F00F500E64

FASTA42946,168
        10         20         30         40         50         60 
MSRSSDLFHK AQTIIPGGVN SPVRAFKGVG GEPVFFKSGK GAYLTDVDDK QYIDYVGSWG 

        70         80         90        100        110        120 
PLILGHCHPK VIEAVDNVLH SGMSFGAPTE LEIQLAEKIA SLMPSIEKIR MVNSGTEATM 

       130        140        150        160        170        180 
TAIRLARGFT NKNKFIKFNG CYHGHSDSLL VKAGSGLLTL GIPSTPGIPQ CITEHTLTAD 

       190        200        210        220        230        240 
FNNLEQVAQL FEKYPNDIAT VILEPVPGNM GFILPKIEFL KGLRELCDQY NALLIFDEVM 

       250        260        270        280        290        300 
TGFRVGLHGA QGLFGIKPDI TTLGKIIGGG MPVGALGGKR EIMSFLAPEG PVYQAGTLSG 

       310        320        330        340        350        360 
NPLAMAAGLA TLKEIEKINF FEDLSSTTNK LTEALSDAAE NANIPLFAAS LGGMFGFCFT 

       370        380        390        400        410        420 
DKNSVENYLD VASSDEVLFK KFFHAMLAQG VYFAPSMYEA GFVSSMHGDL EIQKTYDAAE 


LVLNQLKSA 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Lens.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628337 Genomic DNA. Translation: CAH15732.1.
RefSeqYP_126838.1. NC_006369.1.

3D structure databases

ProteinModelPortalQ5WWG1.
SMRQ5WWG1. Positions 33-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297245.lpl1492.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH15732; CAH15732; lpl1492.
GeneID3115208.
KEGGlpf:lpl1492.
PATRIC22316671. VBILegPne33733_1662.

Organism-specific databases

LegioListlpl1492.
CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycLPNE297245:GJD4-1610-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_LEGPL
AccessionPrimary (citable) accession number: Q5WWG1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 23, 2004
Last modified: February 19, 2014
This is version 70 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