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Q0ST19 (GSA_CLOPS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:CPR_1419
OrganismClostridium perfringens (strain SM101 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier289380 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length425 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 – 425425Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000300903

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0ST19 [UniParc].

Last modified September 19, 2006. Version 1.
Checksum: A1FC7E498ABD03C0

FASTA42546,972
        10         20         30         40         50         60 
MDRNKEIFEE SKKYMPGGVN SPVRSFGSVG INPPVIKSGK GAMIKDENGN EYIDFVLAWG 

        70         80         90        100        110        120 
PMILGHCDED VVEAIKKTSE ESIAFGASTK LELDLAKILC ETLDNVDMIR MVNSGTEATM 

       130        140        150        160        170        180 
SAVKLARGYT KKDKIIKFAG CYHGHFDGFL IEAGSGVLTE GIPGCLGVPE ESIKNTLIGI 

       190        200        210        220        230        240 
YNDEKQVEEL FEKYGNDIAG IIIEPVAGNM GVVKCDPKFM RKLRELCDKY EALLIFDEVM 

       250        260        270        280        290        300 
CGFRVAYKGA QTLFDVKPDL VTYAKIMGGG LPCGAYGGRR EIMENLSPLG GVYQAGTMSG 

       310        320        330        340        350        360 
NPIVMSAGLA TVKKLYENPS YYDHIEKIGS KLEKGIIEIA KKKGLGLVVN RQGGMMTLFF 

       370        380        390        400        410        420 
TDLKEVKCYD DVKTCDGERF KRYFLHMLNK GFNIPPSQFE AMFLSVKHTE EHIDKFLEAF 


ESFEG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000312 Genomic DNA. Translation: ABG87795.1.
RefSeqYP_698738.1. NC_008262.1.

3D structure databases

ProteinModelPortalQ0ST19.
SMRQ0ST19. Positions 3-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING289380.CPR_1419.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG87795; ABG87795; CPR_1419.
GeneID4205980.
KEGGcpr:CPR_1419.
PATRIC19491129. VBICloPer122123_1394.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAHGHANAF.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycCPER289380:GI76-1432-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_CLOPS
AccessionPrimary (citable) accession number: Q0ST19
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 19, 2006
Last modified: May 14, 2014
This is version 56 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