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B0BBJ0 (GSA_CHLTB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:CTLon_0457
OrganismChlamydia trachomatis serovar L2b (strain UCH-1/proctitis) [Complete proteome] [HAMAP]
Taxonomic identifier471473 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length422 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 – 422422Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000121869

Amino acid modifications

Modified residue2581N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0BBJ0 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 966AE029D1A07411

FASTA42245,940
        10         20         30         40         50         60 
MSHLFSKACQ YFPGGVNSPV RACRAVNITP PIVARASKEV FIDSLDKTFI DFCGSWGSLI 

        70         80         90        100        110        120 
HGHSHPKICA AIRQGLERGS SYGLTSEQEI LFAEEIFSYL GLETNYKIRF MSTGSEATMT 

       130        140        150        160        170        180 
AVRLARGITG RPIIIKFLGC YHGHADTFLQ EKPFSHTSLD TLDLAHPLTL SLPFNDFPLF 

       190        200        210        220        230        240 
QTVMNSLGHK VAGVIFEPVC ANMGVILPVP DFIEGVIQTC QQTGSFSIMD EVVTGFRVAQ 

       250        260        270        280        290        300 
GGAAALYHVK PDILVFGKIL GGGLPASAVV APKDIMDHLA PEGKIFQAGT LSGNPLAMIA 

       310        320        330        340        350        360 
GKVSVNLCRE QGFYTQLATI EQNFLSPIEH MIRTTGIPVT LVRYGSLFSF FFNPNRPNNL 

       370        380        390        400        410        420 
ADAQLSDIEA FQKFYQSAFS KGVYLSPSPF EASFLSAAHS MESLDYAQTA LIESLEQVFS 


LV 

« Hide

References

[1]"Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates."
Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D., Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.
Genome Res. 18:161-171(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UCH-1/proctitis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM884177 Genomic DNA. Translation: CAP06855.1.
RefSeqYP_001653550.1. NC_010280.2.

3D structure databases

ProteinModelPortalB0BBJ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING471473.CTLon_0457.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP06855; CAP06855; CTLon_0457.
GeneID5859653.
KEGGctl:CTLon_0457.
PATRIC20382531. VBIChlTra68089_0499.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycCTRA471473:GHJK-484-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]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00713. hemL. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_CHLTB
AccessionPrimary (citable) accession number: B0BBJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 26, 2008
Last modified: May 14, 2014
This is version 52 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