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A6QI46 (GSA2_STAAE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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 2

Short name=GSA 2
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 2
Short name=GSA-AT 2
Gene names
Name:hemL2
Ordered Locus Names:NWMN_1756
OrganismStaphylococcus aureus (strain Newman) [Complete proteome] [HAMAP]
Taxonomic identifier426430 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length429 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 – 429429Glutamate-1-semialdehyde 2,1-aminomutase 2 HAMAP-Rule MF_00375
PRO_0000382378

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6QI46 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 9FD547B0DBD1FD3A

FASTA42946,756
        10         20         30         40         50         60 
MNFSESERLQ QLSNEYILGG VNSPSRSYKA VGGGAPVVMK EGHGAYLYDV DGNKFIDYLQ 

        70         80         90        100        110        120 
AYGPIITGHA HPHITKAIQE QAAKGVLFGT PTELEIEFSK KLRDAIPSLE KIRFVNSGTE 

       130        140        150        160        170        180 
AVMTTIRVAR AYTKRNKIIK FAGSYHGHSD LVLVAAGSGP SQLGSPDSAG VPESVAREVI 

       190        200        210        220        230        240 
TVPFNDINAY KEAIEFWGDE IAAVLVEPIV GNFGMVMPQP GFLEEVNEIS HNNGTLVIYD 

       250        260        270        280        290        300 
EVITAFRFHY GAAQDLLGVI PDLTAFGKIV GGGLPIGGYG GRQDIMEQVA PLGPAYQAGT 

       310        320        330        340        350        360 
MAGNPLSMKA GIALLEVLEQ DGVYEKLDSL GQQLEEGLLK LIEKHNITAT INRIYGSLTL 

       370        380        390        400        410        420 
YFTDEKVTHY DQVEHSDGEA FGKFFKLMLN QGINLAPSKF EAWFLTTEHT EEDIKQTLKA 


ADYAFSQMK 

« Hide

References

[1]"Genome sequence of Staphylococcus aureus strain Newman and comparative analysis of staphylococcal genomes: polymorphism and evolution of two major pathogenicity islands."
Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.
J. Bacteriol. 190:300-310(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Newman.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009351 Genomic DNA. Translation: BAF68028.1.
RefSeqYP_001332790.1. NC_009641.1.

3D structure databases

ProteinModelPortalA6QI46.
SMRA6QI46. Positions 1-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING426430.NWMN_1756.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF68028; BAF68028; NWMN_1756.
GeneID5331044.
KEGGsae:NWMN_1756.
PATRIC19587218. VBIStaAur133992_1898.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAITINRLK.
OrthoDBEOG6QVRHN.
ProtClustDBPRK12389.

Enzyme and pathway databases

BioCycSAUR426430:GIXC-1815-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 nameGSA2_STAAE
AccessionPrimary (citable) accession number: A6QI46
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 54 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