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Q83FJ5 (GSA_TROWT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 78. 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:TWT_729
OrganismTropheryma whipplei (strain Twist) (Whipple's bacillus) [Complete proteome] [HAMAP]
Taxonomic identifier203267 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeTropheryma

Protein attributes

Sequence length466 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 – 466466Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243641

Amino acid modifications

Modified residue2921N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83FJ5 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 76A75C29AE74C473

FASTA46649,582
        10         20         30         40         50         60 
MRTNFEWFEE AKRFIPGGVN SPVRAYAAVG GTPRFLAKAQ GAYVTDIEGR EYVDLVSSWG 

        70         80         90        100        110        120 
PLILGHAHPK VIDAVINTAH RGMSYGAPTT LEVELAELVC NRICNAQGIK PVERLRLVST 

       130        140        150        160        170        180 
GTESCMTAIR LARCFTGRDL IVKFSGHYHG HADPFLIDAG SGLVGHPSSG GVPESVAKNT 

       190        200        210        220        230        240 
LVVPYNDLAV LEYLFEAYPN QIACIITEAC PANMGVIPPD PGFNARVADL GHSHGALIIF 

       250        260        270        280        290        300 
DEVITGFRVG SGGFWALETS LASQQPTQAV SEGSVSDSAY SAYVPDLFTF AKVLGGGLPI 

       310        320        330        340        350        360 
GAIGGRAEIM DLLSPSGPVY QAGTLSGNPL ATAAGLATLR LADSNIYEHM NRVARALINE 

       370        380        390        400        410        420 
IQSAFHDAGV PCTVQSAGNL FGISFSAIAP RDFTQATSQE HWRYSNFFHS MLNSGVLLPP 

       430        440        450        460 
SVYEAWFVSA AFDDRAIERV VNALPDAVRA AGSAPARPKG FEPPTF 

« Hide

References

[1]"Tropheryma whipplei twist: a human pathogenic Actinobacteria with a reduced genome."
Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M., Claverie J.-M.
Genome Res. 13:1800-1809(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Twist.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014184 Genomic DNA. Translation: AAO44826.1.
RefSeqNP_787857.1. NC_004572.3.

3D structure databases

ProteinModelPortalQ83FJ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203267.TWT729.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO44826; AAO44826; TWT_729.
GeneID1482174.
KEGGtwh:TWT729.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycTWHI203267:GJDK-779-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. 2 hits.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGSA_TROWT
AccessionPrimary (citable) accession number: Q83FJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 78 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