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Q2YTC2 (GSA1_STAAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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 1

Short name=GSA 1
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1
Short name=GSA-AT 1
Gene names
Name:hemL1
Ordered Locus Names:SAB1527c
OrganismStaphylococcus aureus (strain bovine RF122 / ET3-1) [Complete proteome] [HAMAP]
Taxonomic identifier273036 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length428 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 – 428428Glutamate-1-semialdehyde 2,1-aminomutase 1 HAMAP-Rule MF_00375
PRO_0000243619

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YTC2 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 6304390735FFEE66

FASTA42846,364
        10         20         30         40         50         60 
MRYTKSEEAM KVAETLMPGG VNSPVRAFKS VDTPAIFMDH GKGSKIYDID GNEYIDYVLS 

        70         80         90        100        110        120 
WGPLILGHRD PQVISHLHEA IDKGTSFGAS TLLENKLAQL VIDRVPSIEK VRMVSSGTEA 

       130        140        150        160        170        180 
TLDTLRLARG YTGRNKIVKF EGCYHGHSDS LLIKAGSGVA TLGLPDSPGV PEGIAKNTIT 

       190        200        210        220        230        240 
VPYNDLDALK IAFEKFGDDI AGVIVEPVAG NMGVIPPIEG FLQGLRDITT EYGALLIFDE 

       250        260        270        280        290        300 
VMTGFRVGYH CAQGYFGVTP DLTCLGKVIG GGLPVGAFGG KKEIMDQIAP LGNIYQAGTL 

       310        320        330        340        350        360 
SGNPLAMTSG YETLSQLAPE TYEYFNMLGD ILEDGLKRVF AKHNVPITVN RAGSMIGYFL 

       370        380        390        400        410        420 
NEGPVTNFEQ ANKSDLKLFA EMYREMAKEG VFLPPSQFEG TFLSTAHTKE DIEKTIQAFD 


TALSRIVK 

« Hide

References

[1]"Molecular correlates of host specialization in Staphylococcus aureus."
Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.
PLoS ONE 2:E1120-E1120(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: bovine RF122 / ET3-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ938182 Genomic DNA. Translation: CAI81216.1.
RefSeqYP_416997.1. NC_007622.1.

3D structure databases

ProteinModelPortalQ2YTC2.
SMRQ2YTC2. Positions 1-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273036.SAB1527c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI81216; CAI81216; SAB1527c.
GeneID3794911.
KEGGsab:SAB1527c.
PATRIC19523951. VBIStaAur92441_1624.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAVATHTIT.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycSAUR273036:GJVS-1549-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 nameGSA1_STAAB
AccessionPrimary (citable) accession number: Q2YTC2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 69 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