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Q2FXR4 (GSA1_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 66. 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
Synonyms:hemL
Ordered Locus Names:SAOUHSC_01771
OrganismStaphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]
Taxonomic identifier93061 [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
Reference 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_0000247015

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict3701Q → T in AAC45836. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q2FXR4 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 88F0566FC5A26D49

FASTA42846,388
        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 IAFEKFGNDI AGVIVEPVAG NMGVVPPIEG FLQGLRDITT EYGALLIFDE 

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

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

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


TALSRIVK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of the Staphylococcus aureus hemCDBL gene cluster coding for early steps in heme biosynthesis."
Kafala B., Sasarman A.
Gene 199:231-239(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The Staphylococcus aureus NCTC 8325 genome."
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
(In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C. (2006)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U89396 Genomic DNA. Translation: AAC45836.1.
CP000253 Genomic DNA. Translation: ABD30840.1.
RefSeqYP_500276.1. NC_007795.1.

3D structure databases

ProteinModelPortalQ2FXR4.
SMRQ2FXR4. Positions 3-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93061.SAOUHSC_01771.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD30840; ABD30840; SAOUHSC_01771.
GeneID3919689.
KEGGsao:SAOUHSC_01771.
PATRIC19580909. VBIStaAur99865_1615.

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycSAUR93061:GIWJ-1690-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_STAA8
AccessionPrimary (citable) accession number: Q2FXR4
Secondary accession number(s): O34092, Q9RL91
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 21, 2006
Last modified: July 9, 2014
This is version 66 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