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P18492 (GSA_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamate-1-semialdehyde 2,1-aminomutase, chloroplastic
Short name=GSA
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name=GSA-AT
Gene names
Name:GSA
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.

Cofactor

Pyridoxal phosphate.

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.

Porphyrin biosynthesis; chlorophyll biosynthesis.

Subunit structure

Homodimer.

Subcellular location

Plastid › chloroplast.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Chloroplast
Chain35 – 469435Glutamate-1-semialdehyde 2,1-aminomutase, chloroplastic
PRO_0000001258

Amino acid modifications

Modified residue3091N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict3091K → Q AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P18492 [UniParc].

Last modified November 1, 1995. Version 3.
Checksum: 78BF03C14A3C1448

FASTA46949,494
        10         20         30         40         50         60 
MAGAAAAVAS GISIRPVAAP KISRAPRSRS VVRAAVSIDE KAYTVQKSEE IFNAAKELMP 

        70         80         90        100        110        120 
GGVNSPVRAF KSVGGQPIVF DSVKGSHMWD VDGNEYIDYV GSWGPAIIGH ADDKVNAALI 

       130        140        150        160        170        180 
ETLKKGTSFG APCALENVLA QMVISAVPSI EMVRFVNSGT EACMGALRLV RAFTGREKIL 

       190        200        210        220        230        240 
KFEGCYHGHA DSFLVKAGSG VATLGLPDSP GVPKGATVGT LTAPYNDADA VKKLFEDNKG 

       250        260        270        280        290        300 
EIAAVFLEPV VGNAGFIPPQ PAFLNALREV TKQDGALLVF DEVMTGFRLA YGGAQEYFGI 

       310        320        330        340        350        360 
TPDVTTLGKI IGGGLPVGAY GGRKDIMEMV APAGPMYQAG TLSGNPLAMT AGIHTLKRLM 

       370        380        390        400        410        420 
EPGTYEYLDK VTGELVRGIL DVGAKTGHEM CGGHIRGMFG FFFAGGPVHN FDDAKKSDTA 

       430        440        450        460 
KFGRFHRGML GEGVYLAPSQ FEAGFTSLAH TTQDIEKTVE AAEKVLRWI

« Hide

References

[1]"Primary structure of a key enzyme in plant tetrapyrrole synthesis: glutamate 1-semialdehyde aminotransferase."
Grimm B.
Proc. Natl. Acad. Sci. U.S.A. 87:4169-4173(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Bonus.
Tissue: Seedling.
[2]"Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and synechococcus."
Grimm B., Bull A., Welinder K.G., Gough S.P., Kannangara C.G.
Carlsberg Res. Commun. 54:67-79(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M31545 mRNA. Translation: AAB59330.1.
PIRA35789.
UniGeneHv.186.

3D structure databases

ProteinModelPortalP18492.
SMRP18492. Positions 47-466.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP18492.

Enzyme and pathway databases

UniPathwayUPA00251; UER00317.
UPA00668.

Gene expression databases

GenevestigatorP18492.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
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.
PTHR11986:SF5. PTHR11986:SF5. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00713. hemL. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_HORVU
AccessionPrimary (citable) accession number: P18492
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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