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A3CL81 (GSA_STRSV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:SSA_0488
OrganismStreptococcus sanguinis (strain SK36) [Complete proteome] [HAMAP]
Taxonomic identifier388919 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length432 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 – 432432Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000079937

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A3CL81 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 19D17EF50ABF9F65

FASTA43246,820
        10         20         30         40         50         60 
MKREHSNQYF TEAQKLFPGG VNSPVRAFKA VGGHPLFIEK ASGAYLHDVD GNRYIDYVLS 

        70         80         90        100        110        120 
WGPMILGHAP KDVLPAVEEA IWEGTSFGAP SPREIALGQL VQERLPFMER MRMVNSGTEA 

       130        140        150        160        170        180 
TMSAIRVARG VTKRSKIVKF IGCYHGHSDS FLVQAGSGLA SFGIADSAGV IAQVAGETLA 

       190        200        210        220        230        240 
LPYNDTDALK TCFEKYGDDI ACVILEAVAG NMGLIPADAD FINTIRSLTQ EYGSLFIVDE 

       250        260        270        280        290        300 
VMSGFRAHYQ GAVGLYQTEP DLVCLGKVIG GGFPVAAFGG KAVYMDQVAP LGSIYQAGTL 

       310        320        330        340        350        360 
SGNPVAMTAG YETLKQLTPE LFAEIEEKTS YLCDGLRSLA DKYSISLQVV SKGTMFGFFF 

       370        380        390        400        410        420 
SQKPVRNFED SKAADHAQFA RLHGLLLEEG IYLAPSQYET NFMSSAHTRA DLDQTLAAFE 

       430 
QAFQEMKEEA NG 

« Hide

References

[1]"Genome of the opportunistic pathogen Streptococcus sanguinis."
Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P., Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D., Paik S., Peterson D.L., Macrina F.L., Buck G.A.
J. Bacteriol. 189:3166-3175(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SK36.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000387 Genomic DNA. Translation: ABN43936.1.
RefSeqYP_001034486.1. NC_009009.1.

3D structure databases

ProteinModelPortalA3CL81.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING388919.SSA_0488.

Proteomic databases

PRIDEA3CL81.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN43936; ABN43936; SSA_0488.
GeneID4807429.
KEGGssa:SSA_0488.
PATRIC19768020. VBIStrSan33173_0472.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAHGHANAF.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycSSAN388919:GHEN-507-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_STRSV
AccessionPrimary (citable) accession number: A3CL81
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 58 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