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Q822Q0 (GSA_CHLCV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 79. 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:CCA_00629
OrganismChlamydophila caviae (strain GPIC) [Complete proteome] [HAMAP]
Taxonomic identifier227941 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length437 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 – 437437Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382292

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q822Q0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 7152AE561D19EF25

FASTA43747,912
        10         20         30         40         50         60 
MPVIDETPMT YTEACRYFPG GVNSPIRACI PVGIVPPIVS SASRDVFIDS FGKNFIDFCG 

        70         80         90        100        110        120 
SWGSLIHGHS HPKILDALCS AASQGTSYGL TSENEISLAT TLFSCLGLQD HKLRFVSSGT 

       130        140        150        160        170        180 
EAAMTSVRLA CGVTQRSVMI KFLGCYHGHA DVLLKGMTID ENNLMEVPHL VDRYFSSDPC 

       190        200        210        220        230        240 
LPLTLILPYN DLKTFEEVME KIGERVACVI FEPIAINMGV VLPEAGWIES IITTCRRYGA 

       250        260        270        280        290        300 
LSIMDEVVTG FRMGSRGMRS ILDVTPDITV YGKILGGGMP VAAVLAHQSI MEHLMPVGTV 

       310        320        330        340        350        360 
FQAGTLSGNP IAMAAGQASI ELCQERDFYP KLENLTEGFL SPIEDFIRCK GFPIALVRAG 

       370        380        390        400        410        420 
SMFSFFFRET PPRNLRDVQE CDQKTFGIFY RHAFSRGVYL SPASMEASFI SSVHSRENLA 

       430 
YTQNVLIDSL VKTFEGI 

« Hide

References

[1]"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G. expand/collapse author list , Rank R.G., Bavoil P.M., Fraser C.M.
Nucleic Acids Res. 31:2134-2147(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GPIC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015925 Genomic DNA. Translation: AAP05371.1.
RefSeqNP_829493.1. NC_003361.3.

3D structure databases

ProteinModelPortalQ822Q0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227941.CCA00629.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP05371; AAP05371; CCA_00629.
GeneID1218314.
KEGGcca:CCA00629.
PATRIC20270373. VBIChlCav107360_0674.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
KOK01845.
OMASQFETIF.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycCCAV227941:GH8L-654-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.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_CHLCV
AccessionPrimary (citable) accession number: Q822Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 79 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